Biochemistry Viva Questions

Cont
actMe@ kar
thi
k.bi
tme@gmai
l.com
Contents
1. Cell Organells ....................................................... 1
2. Cell Membranes: Structure and Function ....... 3
3. Amino Acids: Structure and Properties ........... 8
4. Proteins: Structure and Function .................... 17
5. Enzymology-I ..................................................... 27
6. Enzymology-II: Iso-Enzymes and

Clinical Enzymology ......................................... 40
7. Methods of Separation & Purification of

Biological Compounds, Methods of
Study of Metabolism ......................................... 47
8. Carbohydrates-I:Chemistry, Digestion and

Absorption .......................................................... 52
9. Carbohydrates-II: Major Metabolic

Pathways of Glucose, Glycolysis,
Gluconeogenesis, Glycogen Metabolism ...... 61
10. Carbohydrates-III: Regulation of Blood

Sugar, Insulin and Diabets Mellitus .............. 70
11. Carbohydrates-IV: Other Metabolic Pathways

(HMP Shunt Pathway, Fructose, Galactose,
Glucuronic Acid, Alcohol) ................................ 81
2 Viva—based on Textbook of Biochemistry
12. Lipids-I: Chemistry, Digestion and

Absorption of Lipids ......................................... 88
13. Lipids-II: Metabolism of Fatty acids, Fatty acid

oxidation, Fatty acid synthesis, Lipolysis,
Ketone bodies ..................................................... 95
14. Lipids-III: Cholesterol, Lipoproteins and

Cardiovascular Diseases ................................. 103
15. Lipids-IV: MCFA, PUFA and

Prostaglandins .................................................. 112
16. Lipids-V: Compound Lipids ......................... 118
17. Amino Acid Metabolism-I:

General: Digestion, Absorption,
Transamination, Urea ...................................... 122
18. Amino Acid Metabolism-II: Simple,

Hydroxy and Sulfur Containing Amino
Acids Glycine, Serine, Alanine, Threonine,
Methionine, Cysteine ...................................... 128
19. Amino Acid Metabolism-III: Acidic, Basic and

Branched Chain Amino Acids, Glutamic acid,
Glutamine, Aspartic acid, Asparagine, Lysine,
Nitric Oxide, Valine, Leucine, Isoleucine .... 132
20. Amino Acid Metabolism-IV: Aromatic Amino

Acids: Phenyl alanine, Tyrosine, Tryptophan,
Histidine ............................................................ 137
21. Amino Acid Metabolism-V: Inter-relations of

Amino Acid Metabolisms, One Carbon
Metabolism, Amino Acidurias ...................... 142
Contents 3
22. Citric Acid Cycle .............................................. 144
23. Electron Transport Chain ............................... 147
24. Free Radicals and Anti-oxidants ................... 151
25. Plasma Proteins ................................................ 153
26. Immunochemistry ............................................ 156
27. Specialised Proteins: Collagen, Myosin ...... 158
28. Heme Synthesis and Breakdown ................. 160
29. Haemoglobins .................................................. 165
30. Vitamin-I: Fat Soluble Vitamins: A, D, E

and K .................................................................. 169
31. Vitamin-II: Water soluble vitamins .............. 174
32. Mineral Metabolism ........................................ 189
33. Energy Metabolism and Nutrition ............... 195
34. Detoxification and Biotransformation of

Xenobiotics ........................................................ 199
35. Biochemical Aspects of Environmental

Pollution ............................................................ 201
36. Acid Base Balance and pH ............................. 203

37. Electrolyte and Water Balance ....................... 207
38. Molecular Biology-I: Nucleotides, Chemistry

and Metabolism ............................................... 209
39. Molecular Biology-II: DNA structure and

Replication ........................................................ 216
40. Molecular Biology-III: Transcription and

Translation ........................................................ 220
41. Molecular Biology-IV: Molecular Genetics

and Control of Gene Expression ................... 227
42. Molecular Biology-V: Recombinant DNA

Technology and Gene Therapy .................... 229
43. Biochemistry of AIDS ..................................... 233
44. Biochemistry of Cancer ................................... 235
45. Applications of Radio-isotopes in

Medicine ............................................................ 238
46. Body Fluids ....................................................... 240
47. Hormones-I: Mechanism of Action of

Hormones .......................................................... 242
48. Hormones-II: Pituitary Hormones ................ 244
49. Hormones-III: Steroid Hormones ................. 246
50. Hormones-IV: Thyroid Hormones ............... 248
51. Clinical Biochemistry-I: .................................. 250

52. Clinical Biochemistry-II: Liver and
Gastric Function Tests ..................................... 252
53. Clinical Biochemistry-III: Kidney Function

Tests .................................................................... 256
Cell Organelles 1
Cell Organelles
Q. What is the function of Golgi complex?

A. Maturation and processing of nascent proteins,
glycosylation of proteins, secretion newly
synthesised proteins (Page 3).
Q. What is the function of endoplasmic reticulum?
(Page 3)
A. Biosynthesis of proteins, drug metabolism,
desaturation of fatty acids.
Q. What is the marker enzyme for endoplasmic
reticulum?
A. Glucose-6-phosphatase (Page 3, Table 1.3).
Q. Where does protein synthesis take place?
A. On the walls of endoplasmic reticulum and also
in cytosol (Page 3).
Q. What are cathepsins?
A. They are intracellular proteolytic enzymes
(Page 4).
Q. What is the function of lysosomes?

A. They are bags of hydrolytic enzymes that bring
about degradation of macromolecules (Page 4).
Q. What is lysozyme?
A. It is an enzyme present in external secretions
(Page 35).
Q. What are peroxisomes?
A. They contain peroxidase and catalase, necessary
for destroying the unwanted free radicals.
(Page 4)
Q. What are the important metabolic events taking
place in cytoplasm?
A. Glycolysis (Embden-Meyerhof pathway), HMP
shunt pathway, glycogen metabolism, Fatty acid
synthesis, Synthesis of nucleotides, Degradation
of amino acids (See Page 5, Table 1.4).
Q. What is the function of mitochondria?
A. Generation of ATP (See page 5).
Q. What are the important metabolic events taking
place in mitochondria?
A. TCA cycle, electron transport chain, beta oxida-
tion of fatty acids and urea cycle (Page 5).
Cell Membranes; Structure and Function 3
Cell Membranes:
Structure and Function
Q. What are ecto-enzymes?

A. They are enzymes seen on the outer part of cell
membrane (Page 6).
Q. Give examples of ecto-enzymes.
A. Alkaline phosphatase, 5’nucleotidase (Page 6).
Q. How do you describe the structure of cell mem-
brane?
A. Fluid mosaic model (Page 6).
Q. What are the characteristics of fluid mosaic
model?.
A. Membrane is composed of lipid bilayer. Phospho-
lipids are arranged in bilayers with a hydropho-
bic core (Page 6).
Q. What do you mean by fluidity of the membrane?
A. The lipid bilayer shows free lateral movement of
its components; but flip-flop movement is re-
stricted (Page 6).
Q. What are the components of membrane that al-

ter the fluidity?
A. Cholesterol and unsaturated fatty acids (Page 6).
Q. What are the different types of transport mecha-
nisms?
A. Passive and active. Passive type is subclassified
as simple diffusion and facilitated diffusion
(Page 8).
Q. What are the salient features of facilitated diffu-
sion?
A. It is carrier mediated. It does not require energy
directly (Page 8).
Q. Can you give an example of facilitated transport?
A. Glucose transporters (Page 8).
Q. What are ion channels?
A. They are special devices for quick transport of
electrolytes (Page 9).
Q. Give some examples of ion channels.
A. Ion channels specific for calcium, potassium and
chloride (Page 9).
Q. What are ionophores?
A. They are transport antibiotics which increase the
permeability of membrane to ions, e.g. valinomy-
cin, gramicidin (Page 10).
Q. What are the salient features of active transport?
A. It requires transporters. It requires energy. Trans-
port is generally unidirectional (Page 10).
Q. Give examples of active transport systems.

A. Sodium pump, calcium pump (Page 10).
Q. What is the importance of sodium pump?
A. Cell has low intracellular sodium; but concentra-
tion of potassium inside the cell is high; this is
maintained by sodium pump. About 40% of the
total energy expenditure in a cell is used for this
active transport system (Page 10).
Q. How does sodium pump work?
A. It is called sodium-potassium activated ATPase.
Hydrolysis of one molecule of ATP can result in
expulsion of 3 sodium ions and influx of 2 potas-
sium ions (Page 10).
Q. What is its clinical significance?
A. Digoxin increases the contractility of the cardiac
muscle, by inhibiting the sodium pump (Page
10).
Q. What is a uniport?
A. It carries single solute across the membrane
(Page 10).
Q. Give examples of uniport.
A. Glucose transporter (GluT2) operating in most of
the cells is an example. Calcium pump is another
example (Page 10).
Q. What is co-transport?
A. If transfer of one molecule depends on simulta-
neous or sequential transfer of another molecule,
it is called co-transport system (Page 10).
Q. How are co-transport systems classified?

A. The cotransport system may be symport or
antiport (Page 10).
Q. What is symport?
A. In symport, the transporter carries two solutes in
the same direction across the membrane (Page
10).
Q. Give examples of symport. (Page 10)
A. Sodium dependent glucose transporter (SgluT)
(Fig.8.31). Phlorhizin, an inhibitor of sodium-de-
pendent cotransport of glucose, especially in the
proximal convoluted tubules of kidney, produces
renal damage and results in renal diabetes. Amino
acid transport is another example for symport.
Q. What is antiport system?. (Page 10)
A. The antiport system carries two solutes or ions in
opposite direction.
Q. Give examples of antiport. (Page 10)
A. Sodium pump (Fig.2.7) or chloride-bicarbonate
exchange in RBC (Fig.29.4).
Q. What is endocytosis?. (Page 11)
A. It is the mechanism by which cells internalise ex-
tracellular macromolecules.
Q. What is pinocytosis?. (Page 11)
A. It is receptor mediated. Low Density Lipoprotein
(LDL) binds to the LDL receptor and the complex
is later internalised. These vesicles are coated with
Clathrin. .
Q. What is phagocytosis. (Page 11)

A. It is the engulfment and internalisation of large
particles such as bacteria by macrophages and
granulocytes.
Q. What is respiratory burst. (Page 11)
A. During phagocytosis, there is an increase in oxy-
gen consumption with formation of the superox-
ide ion.
Amino Acids:
Structure and
Properties
Q. How do you classify amino acids? (Page 12)

A. Based on the structure, amino acids are classified
into: Simple amino acids, Branched chain amino
acids, Hydroxy amino acids, Sulfur containing
amino acids, Amino acids with amide group,
Acidic amino acids, Basic amino acids, Aromatic
amino acids, Heterocyclic amino acids, Imino acid
and Derived amino acids.
Q. What are branched chain amino acids?(Page 12)
A. Valine, leucine and isoleucine.
Q. What are hydroxy amino acids? (Page 12)
A. Serine and threonine.
Q. Name the Sulfur containing amino acids.
(Page 12)
A. Cysteine and methionine.
Q. Name the acidic amino acids. (Page 12)
A. Aspartic acid and glutamic acid.
Amino Acids: Structure and Properties 9
Q. What are the basic amino acids? (Page 12)

A. Lysine and arginine.
Q. Which amino acid has a net positive charge at
physiological pH? (Page 12)
A. Arginine and lysine.
Q. Amino acid containing a thio-ether bond is.
(Page 12)
A. Methionine.
Q. Give examples of amino acids with hydropho-
bic side chains. (Page 12)
A. Valine, leucine, isoleucine.
Q. Give the names of aromatic amino acids.
(Page 12)
A. Phenylalanine and tyrosine.
Q. What are heterocyclic amino acids? (Page 12)
A. Tryptophan and histidine.
Q. Give an example of an imino acid. (Page 12)
A. Proline.
Q. Give examples of derived amino acids.(Page 12)
A. Hydroxy proline, hydroxy lysine, ornithine, cit-
rulline, homocysteine.
Q. Arginine contains which special group?
(Page 12)
A. Guanidinium group (-NH-CNH-NH2).
Q. Benzene group is present in which amino acid?
(Page 12)
A. Phenyl alanine.
Q. Phenol group is present in which amino acid?

(Page 12)
A. Tyrosine.
Q. Tryptophan contains what special group?
(Page 12)
A. Indole group.
Q. Which special group is present in Histidine?
(Page 12)
A. Imidazole group.
Q. Name some hydrophobic amino acids.(Page 12)
A. Valine, leucine and isoleucine.
Q. Pyrrolidine group is present in which amino
acid? (Page 12)
A. Proline.
Q. Hydrophobic bonds are formed in protein be-
tween which amino acids?
A. Valine, leucine and isoleucine residues.(Page 12)
Q. What is the basis of classification of amino acids
into ketogenic and glucogenic?
(Page 12 and 13)
A. Ketogenic amino acids enter into the metabolic
pathway of fats, while glucogenic amino acids
enter the pathway of glucose metabolism.
Q. Name a purely ketogenic amino acid.
(Page 12)
A. Leucine.
Q. Name some glucogenic amino acids. (Page 13)
A. Glycine; serine; aspartic acid.
Q. Which amino acid is synthesised after it gets in-

corporated into the protein?
A. Hydroxyproline (Page 12).
Q. What are essential amino acids? (Page 13)
A. They cannot be synthesized in the body; and so,
they are to be provided in the diet.
Q. How many amino acids are essential? (Page 13)
A. Eight amino acids are essential; two are semi-es-
sential and the rest 10 are non-essential.
Q. Are non-essential amino acids necessary for the
body?
A. They are also necessary for protein synthesis, but
they can be synthesized by the body and need
not be essentially present in the diet (Page 14).
Q. Name any three essential amino acids. (Page 13)
A. Isoleucine, leucine, threonine.
Q. Is phenyl alanine an essential amino acid?
(Page 13)
A. Yes.
Q. What about Tyrosine? (Page 13)
A. Tyrosine is non-essential, it is synthesized from
phenyl alanine.
Q. Name the semi-essential amino acids. (Page 14)
A. Histidine and arginine.
Q. Why are they called semi-essential? (Page 14)
A. Because growing children require them in food.
But they are not essential for the adult individual.
Q. What is iso-electric point?. (Page 14)

A. The pH at which the molecule carries no net charge
is called iso-electric point.
Q. What are the characteristic features of iso-elec-
tric pH. (Page 14)
A. At iso-electric point the amino acid will carry no
net charge, there is no mobility in electrical field,
solubility will be minimum, the tendency for pre-
cipitation will be maximum
Q. What is the speciality of Histidine? (Page 14)
A. The pK value of Histidine is 6.1, and therefore
effective as a buffer at the physiological pH of 7.4.
The buffering capacity of plasma proteins and
hemoglobin is mainly due to histidine residue.
Q. Which is the amino acid having maximum buff-
ering capacity at physiological pH? (Page 14)
A. Histidine.
Q. Which amino acid is optically inactive?
(Page 15)
A. Glycine.
Q. What are the isomers of amino acids? (Page 16)
A. D and L varieties.
Q. What are natural amino acids? (Page 16)
A. Only L amino acids are seen in large quantities in
nature.
Q. Can you name some substances where D-amino

acids are seen?
A. D-amino acids are seen in cell walls of micro-or-
ganisms and as constituents of certain antibiotics
such as gramicidin-S, polymyxin, actinomycin-D
and valinomycin (Page 16).
Q. What is meant by decarboxylation of an amino
acid? (Page 16)
A. The carboxyl group is removed from the amino
acids to form the corresponding amine (Fig.3.8).
Q. Give examples of decarboxylation reactions.
(Page 16)
A. Histidine to histamine; tyrosine to tyramine; tryp-
tophan to tryptamine.
Q. What is produced when Glutamic acid is decar-
boxylated? (Page 16)
A. Gamma amino butyric acid or GABA.
Q. What is glutamine? (Page 16)
A. That is the amide of glutamic acid.
Q. What is an amide? (Page 16)
A. The extra carboxyl group (other thanÿalpha car-
boxyl) can combine with ammonia to form the cor-
responding amide.
Q. How asparagines is produced? (Page 16)
A. Aspartic acid + ammonia will form asparagine.
Q. What is transamination? (Page 16)
A. The alpha amino group of amino acid can be trans-
ferred to alpha keto acid to form the correspond-
ing new amino acid and alpha keto acid (Fig.3.10).
Q. Give an example of transamination reaction.

(Page 16)
A. Glutamic acid + pyruvic acid alpha keto glutarate
+ alanine.
Q. What is the product of transamination reaction
of pyruvate with glutamate?
A. Alanine and alpha keto glutarate (Page 16).
Q. What is the biological significance of transami-
nation reaction?
A. These are important for the interconversion of
amino acids. Non-essential amino acids are syn-
thesized by this process (Page 16).
Q. What is the clinical significance of transami-
nases? (Page 16)
A. Transaminases in blood are elevated in liver and
heart diseases.
Q. What is the significance of SH groups in pro-
teins? (Page 17)
A. The SH group of cysteine can form a disulfide (S-
S) bond with another cysteine residue. The two
cysteine residues can connect two polypeptide
chains by the formation of interchain disulfide
bonds.
Q. Glutathione is made up of which amino acids?
(Page 17)
A. Glutamic acid, cysteine and glycine.
Q. Phosphorylation is taking place on which amino
acid residue?
A. Serine (Page 17).
Q. What is ninhydrin reaction? (Page 18)

A. All amino acids when heated with ninhydrin will
give a pink colour.
Q. What is the importance of ninhydrin reaction?
(Page 18)
A. It is used for qualitative test and quantitative es-
timation of amino acids. It is often used for detec-
tion of amino acids in chromatography.
Q. Do proteins give a color with ninhydrin?
(Page 18)
A. Proteins do not give a true color reaction; but N-
terminal end amino group of protein will react
with ninhydrin, to produce a blue color.
Q. What is biuret reaction? (Page 18)
A. Cupric ions in alkaline medium form a violet
colour with peptide bond nitrogen.
Q. Will amino acids give a positive biuret test?
(Page 18)
A. No. This needs a minimum of two peptide bonds.
Q. What is the use of biuret reaction? (Page 18)
A. This reaction can be used for qualitative identifi-
cation and quantitative estimation of proteins.
Q. What is biuret? (Page 18)
A. The name is derived from the compound biuret,
a condensation product of two urea molecules,
which also gives a positive color test.
Q. What is the basis of xanthoproteic test?

(Page 18)
A. The ring systems in phenyl alanine, tyrosine and
tryptophan will answer this test.
Q. The protein which does not answer the aldehyde
test is. (Page 18)
A. Gelatin.
Proteins: Structure and Function 17
Proteins: Structure
and Function
Q. How proteins are made up of? (Page 19)

A. Proteins are made by polymerisation of amino
acids through peptide bonds.
Q. What is a peptide bond? (Page 19)
A. Alpha carboxyl group of one amino acid reacts
with alpha amino group of another amino acid to
form a peptide bond or CO-NH bridge (Fig. 4.1).
Q. What is a dipeptide? (Page 19)
A. Two amino acids are combined to form a dipep-
tide.
Q. How many peptide bonds are present in a trip-
eptide? (Page 19)
A. A tripeptide is a combination of three amino ac-
ids; so there are two peptide bonds.
Q. What is a polypeptide? (Page 19)
A. A combination of 10 to 50 amino acids is called as
a polypeptide.
Q. What is the difference between a polypeptide

and a protein? (Page 19)
A. A combination of 10 to 50 amino acids is called a
polypeptide. By convention, chains containing
more than 50 amino acids are called proteins.
Q. What are the levels of organizations of proteins?
(Page 19)
A. Proteins have primary, secondary, tertiary and
quaternary levels of organisation.
Q. What is meant by primary structure of a protein?
(Page 19)
A. It denotes the number and sequence of amino ac-
ids in the protein.
Q. What is the force that maintains the primary
structure? (Page 19)
A. The primary structure is maintained by the cova-
lent bonds of the peptide linkages (Fig. 4.2).
Q. What are the salient features of a peptide bond?
(Page 19)
A. The peptide bond is a partial double bond. The
C-N bond is ‘trans’ in nature and there is no free-
dom of rotation because of the partial double bond
character.
Q. What is the N-terminal end of a protein?
(Page 20)
A. In a protein, at one end there will be one free al-
pha amino group. This end is called the amino
terminal (N-terminal) end and the amino acid con-
tributing the ?-amino group is named as the first
amino acid.
Q. What are the names for the end amino acids of

proteins. (Page 20)
A. The end where there is a free alpha amino group
is called the amino terminal (N-terminal) end. The
other end of the polypeptide chain is called the
carboxy terminal end (C-terminal) where there is
a free alpha carboxyl group.
Q. Can you give an example of a pseudopeptide?
(Page 20)
A. Glutathione (gamma-glutamyl-cysteinyl-glycine).
The pseudopeptide a peptide bond formed by
carboxyl group, other than that of alpha position.
Q. What are the salient structural features of insu-
lin? (Page 20)
A. It has two polypeptide chains. These chains are
held together by disulfide bridges. Insulin has
total 51 amino acids.
Q. What is pro-insulin? (Page 20)
A. Insulin is synthesised by the beta cells of pancreas
as a prohormone, proinsulin is a single poly-pep-
tide chain with 86 amino acids.
Q. What is mutation? (Page 20)
A. Amino acid change in the linear sequence is called
a mutation.
Q. Can you give an example? (Page 20)
A. sickle cell anemia due to Haemoglobin S,
Q. What is the defect in HbS? (Page 20)
A. Normally the 6th amino acid in the beta chain is
glutamic acid, this is replaced by valine in the HbS
molecule.
Q. Which are the forces that maintain the second-

ary, tertiary and quaternary structures of a pro-
tein? (Page 21)
A. Hydrogen bonds, Electrostatic bonds, Van der
Waal’s forces and Hydrophobic bonds.
Q. What are the salient features of alpha structure
of proteins? (Page 22)
A. It is a right-handed spiral structure; each turn is
formed by 3.6 amino acid residues; it is major
structural motif in globular proteins.
Q. Which will inhibit the formation of alpha helix?
(Page 22)
A. Proline.
Q. What is meant by secondary structure of a pro-
tein? (Page 22)
A. Secondary structure denotes the configurational
relationship between residues which are about 3-
4 amino acids apart. In other words, secondary
level defines the organisation at immediate vicin-
ity of amino acids.
Q. What is meant by tertiary structure of a protein?
(Page 22)
A. The tertiary structure denotes three dimensional
structure of the whole protein. It defines the steric
relationship of amino acids which are far apart
from each other in the linear sequence.
Q. What is meant by a domain of a protein?
(Page 22)
A. It is the term used to denote a compact unit of a
protein. It generally represents a functional unit.
Q. What is meant by quaternary structure of a pro-

tein? (Page 22)
A. Certain polypeptides will aggregate to form one
functional protein. This is referred to as the qua-
ternary structure.
Q. Give some examples of proteins having quater-
nary structure. (Page 23)
A. Hemoglobin, lactate dehydrogenase, immunoglo-
bulin.
Q. What are the reagents that are used for identify-
ing the first amino acid in a protein? (Page 24)
A. Fluoro dinitro benzene, dansyl chloride, phenyl
iso thio cyanate.
Q. Protein chains may be separated by what re-
agent? (Page 24)
A. 8 molar urea.
Q. What is meant by Ingram’s technique?(Page 24)
A. Protein digestion by trypsin, followed by two di-
mensional chromatography.
Q. It is otherwise known as what? (Page 24)
A. Finger printing of proteins or peptide mapping.
Q. Secondary structure of protein can be studied by
what methods? (Page 25)
A. X-ray diffraction study, optical rotatory disper-
sion, and nuclear magnetic resonance (NMR).
Q. What is iso-electric point of a protein? (Page 25)
A. At the iso-electric point, the number of anions and
cations present on the protein molecule will be
equal and the net charge is zero.
Q. What are the characteristic features of iso-elec-

tric point? (Page 25)
A. At the pI value, the proteins will not migrate in
an electrical field; solubility, buffering capacity
and viscosity will be minimum and precipitation
will be maximum.
Q. What is the iso-electric pH of human albumin?
(Page 25)
A. It is 4.7.
Q. How proteins are precipitated from solution?
(Page 25)
A. Any factor which neutralises the charge or re-
moves water of hydration will cause precipita-
tion of proteins.
Q. How albumin is precipitated? (Page 25)
A. By full saturation of ammonium sulfate or 28 %
sodium sulfate.
Q. What will be precipitated by half-saturation of
ammonium sulfate? (Page 25)
A. Globulins are precipitated by half-saturation of
ammonium sulfate.
Q. Give an example of precipitation at iso-electric
point. (Page 26)
A. Casein is precipitated when the solution is
brought to iso-electric pH.
Q. What is the iso-electric pH of casein? (Page 26)
A. 4.6.
Q. Give some examples of anionic precipitating

agents. (Page 26)
A. Tungstic acid, phosphotungstic acid, trichloro
acetic acid, picric acid, sulphosalicylic acid and
tannic acid are protein precipitating agents.
Q. What are the features of denaturation?(Page 26)
A. The secondary, tertiary and quaternary structures
are lost, but primary structure is preserved. The
functional activity is lost. The denature proteins
are insoluble and easily precipitated.
Q. What are the usual agents that cause denaturation
of proteins? (Page 26)
A. Brief heating, urea, X-ray, ultraviolet ray, high
pressure, vigorous shaking.
Q. What is heat coagulation? (Page 26)
A. When heated at iso-electric point, some proteins
will denature irreversibly to produce thick float-
ing conglomerates called coagulum. This is called
heat coagulation.
Q. Give examples of proteins that coagulate easily.
(Page 26)
A. Albumin is easily coagulated, and globulins to a
lesser extent.
Q. How proteins are classified? (Page 27)
A. They may be classified depending on the func-
tion or based on the physicochemical characteris-
tics or based on their nutritional value.
Q. What is the functional classification of proteins?

(Page 27)
A. 1. Catalytic proteins, 2. Structural proteins, 3. Con-
tractile proteins, 4. Transport proteins, 5. Regula-
tory proteins or hormones, 6. Genetic proteins,
and 7. Protective proteins.
Q. Based on physiochemical properties, how are
they classified? (Page 27)
A. Simple proteins, conjugated proteins and derived
proteins.
Q. Give examples of simple proteins. (Page 27)
A. Albumins, globulins, protamines, prolamines,
lectins, scleroproteins.
Q. Give examples of scleroproteins. (Page 27)
A. Collagen of bone, cartilage and tendon, keratin of
hair, horn, nail and hoof.
Q. What are conjugated proteins? (Page 27)
A. Combinations of protein with a non-protein part
is called prosthetic group.
Q. How are conjugated group subclassified?
(Page 27)
A. Glycoproteins, lipoproteins, nucleoproteins, chro-
moproteins, phospho-proteins and metallo-pro-
teins.
Q. Give some examples of chromoproteins.
(Page 27)
A. Hemoglobin, flavoproteins, visual purple.
Q. Give examples of phosphoproteins.

(Page 27)
A. Casein of milk and vitellin of egg yolk.
Q. Where is this phosphate attached to proteins?
(Page 27)
A. The phosphoric acid is added to the hydroxyl
groups of serine and threonine residues of pro-
teins.
Q. What are lectins? (Page 27)
A. Plant proteins having specific carbohydrate bind-
ing site.
Q. Give an example of a nutritionally rich protein
(first class protein). (Page 28)
A. Casein.
Q. Some proteins are called as poor proteins; why?
(Page 28)
A. They lack in many essential amino acids and a
diet based on these proteins will not even sustain
the body weight.
Q. Give an example of nutritionally poor protein.
(Page 28)
A. Zein from corn lacks tryptophan and lysine.
Q. Which method of protein estimation is depen-
dent on the intact peptide bond?
A. Biuret method. (Page 28)
Q. What is the advantage of biuret method?

(Page 28)
A. The biuret method is simple one step process, and
is the most widely used method for plasma pro-
tein estimations.
Q. What is the disadvantage of biuret method?
(Page 28)
A. The sensitivity of the method is less and is un-
suitable for estimation of proteins in milligram
or microgram quantities.
Q. What is the basis of Lowry’s method of protein
estimation? (Page 28)
A. This is based on the reduction of folin-ciocalteau
phenol reagent (phosphomolybdic acid and phos-
photungstic acid) by the tyrosine and tryptophan
residues of protein.
Q. Which component of the protein absorb UV light
at 280 nm? (Page 28)
A. Indole ring of tryptophan.
Q. What is nephelometry? (Page 29)
A. Nephelometry is defined as the detection of light
scattered by turbid particles in solution.
Enzymology-I 27
Enzymology-I
Q. How are enzymes classified? (Page 30)

A. They are classified into five major classes.
Q. What are those classes? (Page 30)
A. Oxidoreductases, transferases, hydrolases, lyases,
isomerases and ligases.
Q. What is the function of oxidoreductases?
(Page 30)
A. Transfer of hydrogen.
Q. Give an example of oxidoreducatase. (Page 30)
A. Alcohol dehydrogenase.
Q. What is the function of transferases? (Page 31)
A. Transfer of groups other than hydrogen.
Q. Give an example of transferase. (Page 31)
A. Hexokinase.
Q. What is the function of hydrolases? (Page 31)
A. Cleave bond after adding water.
Q. Give an example of a hydrolase. (Page 31)

A. Acetyl choline esterase.
Q. Peptidases are classified under which class of
enzyme? (Page 31)
A. Hydrolases.
Q. What is the function of lyases? (Page 31)
A. Cleave bond without adding water.
Q. Which enzyme will add water to a double bond,
without breaking the bond?
A. Hydratase. (Page 31)
Q. Give an example of lyase. (Page 31)
A. Aldolase.
Q. Give an example of isomerase. (Page 31)
A. Triose phosphate isomerase.
Q. What is the function of ligases? (Page 31)
A. ATP dependent condensation of two molecules.
Q. What is the difference between synthase and syn-
thetase? (Page 31)
A. Synthetases are ATP-dependent enzymes
catalysing biosynthetic reactions; they belong to
Ligases. Synthases are enzymes catalysing biosyn-
thetic reactions; but they do not require ATP di-
rectly; they belong to classes other than Ligases.
Q. Give examples of synthetases. (Page 31)
A. Carbamoyl phosphate synthetase, arginino suc-
cinate synthetase, PRPP synthetase, glutamine
synthetase.
Enzymology-I 29
Q. Give examples of synthases. (Page 31)

A. Glycogen synthase, ALA synthase, IMP synthase.
Q. What are co-enzymes? (Page 31)
A. Enzyme may contain a non-protein part, the co-
enzyme. The co-enzyme is essential for the bio-
logical activity of the enzyme. A co-enzyme is a
low molecular weight organic substance, without
which the enzyme cannot exhibit any reaction. Co-
enzyme accepts one of the products of the reac-
tion; and so act as a co-substrate.
Q. What is holo-enzyme? (Page 31)
A. When apo-enzyme and co-enzymes are added,
holo-enzyme is produced. Fully active enzyme
is called Holo-enzyme.
Q. How are co-enzymes classified? (Page 31)
A. (a) Those taking part in reactions catalysed by oxi-
doreductases by donating or accepting hydrogen
atoms or electrons. (b) Those co-enzymes taking
part in reactions transferring groups other than
hydrogen.
Q. Give some examples of co-enzymes involved in
oxidoreductases. (Page 31)
A. NAD, NADP, FAD.
Q. What is the full form of NAD? (Page 32)
A. Nicotinamide adenine dinucleotide.
Q. What is FAD? (Page 32)
A. Flavin adenine dinucleotide.
Q. Give some examples of co-enzymes involved in

reactions other than hydrogen transfer.
(Page 32)
A. Thiamine pyrophosphate, pyridoxal phosphate,
biotin, co-enzyme A, ATP.
Q. What is the full form of ATP? (Page 32)
A. Adenosine triphosphate.
Q. What is the function of ATP? (Page 32)
A. It is the energy currency in the body. During the
oxidation of food stuffs, energy is released, a part
of which is stored as chemical energy in the form
of ATP. Other reaction requiring energy are
coupled with ATP.
Q. Name the enzymes containing copper.(Page 33)
A. Superoxide dismutase, tyrosinase, cytochrome
oxidase.
Q. Which metal is required for the action of Kinases?
(Page 33)
A. Magnesium.
Q. Chloride ions activate which enzyme? (Page 33)
A. Amylase.
Q. Which enzyme contains molybdenum?
(Page 33)
A. Xanthine oxidase.
Q. Name some iron containing enzymes. (Page 33)
A. Cytochrome oxidase, catalase, peroxidase, xan-
thine oxidase.
Enzymology-I 31
Q. What is Michaelis-Menten Theory ? (Page 33)

A. It is otherwise called enzyme-substrate complex
theory. The enzyme combines with the substrate,
to form an enzyme-substrate complex, which im-
mediately breaks down to the enzyme and the
product.
Q. What is Fischer’s theory? (Page 34)
A. It states that the three dimensional structure of
the active site of the enzyme is complementary to
the substrate. Thus, enzyme and substrate fit each
other like a key and its lock.
Q. What is Koshland’s induced fit theory?
(Page 34)
A. The substrate induces conformational changes in
the enzyme, such that precise orientation of cata-
lytic groups is effected.
Q. What is active site of an enzyme? (Page 35)
A. That area of the enzyme where catalysis occurs is
referred to as active site or active center.
Q. What is meant by serine proteases? (Page 35)
A. Proteases (proteolytic enzymes) having a serine
residue at its active center.
Q. Give an example of a serine protease. (Page 35)
A. Trypsin, chymotrypsin, thrombin.
Q. Thermodynamically, how reactions are classi-
fied? (Page 36)
A. Exothermic, isothermic and endothermic reac-
tions.
Q. What is exothermic reaction? (Page 36)

A. Here energy is released from the reaction, and
therefore reaction essentially goes to completion,
e.g. urease enzyme, converting urea to ammonia
+ CO2 + energy.
Q. What is endergonic reaction? (Page 36)
A. Energy is consumed and external energy is to be
supplied for these reactions. In the body this is
usually accomplished by coupling the endergonic
reaction with an exergonic reaction, e.g. Hexoki-
nase reaction, Glucose + ATP ® Glucose-6-Phos-
phate + ADP.
Q. What are the salient features of enzyme kinet-
ics? (Page 36)
A. Enzymes lower activation energy. They increase
the chemical reaction, but do not alter equilibrium
of the reaction.
Q. What are the factors influencing enzyme reac-
tion? (Page 36)
A. Enzyme concentration, substrate concentration,
product concentration, temperature, pH and pres-
ence of activators or inhibitors.
Q. What is Km value? (Page 37)
A. Substrate concentration (expressed in moles/L)
at half-maximal velocity is the Km value.
Q. What does it indicate? (Page 37)
A. It denotes that 50% of enzyme molecules are
bound with substrate molecules at that particu-
lar substrate concentration
Enzymology-I 33
Q. What is its significance? (Page 37)

A. Km is independent of enzyme concentration. Km
value is thus constant for an enzyme. It is the char-
acteristic feature of a particular enzyme for a spe-
cific substrate. Km denotes the affinity of enzyme
to substrate. Thus, the lesser the numerical value
of Km, the affinity of the enzyme for the substrate
is more.
Q. What is the use of assessing the Km value of an
enzyme? What is the application? (Page 38)
A. Determination of Km value is also useful to un-
derstand the natural substrate of an enzyme. Study
of Km value will also differentiate the competi-
tive and non-competitive inhibitions.
Q. What is the effect of temperature on enzyme ve-
locity? (Page 39)
A. The velocity of reaction increases when tempera-
ture is increased, reaches a maximum and then
falls (Bell-shaped curve)
Q. Why it falls? (Page 39)
A. when temperature is more than 50ºC, heat dena-
turation and consequent loss of tertiary structure
of protein occurs.
Q. What is the effect of pH on the activity of an en-
zyme? (Page 39)
A. Each enzyme has an optimum pH, on both sides
of which the velocity will be drastically reduced.
The graph will show a bell-shaped curve.
Q. What is the explanation for the effect of pH?

(Page 39)
A. The pH decides the charge on the amino acid resi-
dues at the active site. The net charge on the en-
zyme protein would influence substrate binding
and catalytic activity.
Q. What is the optimum pH of usual enzymes?
(Page 39)
A. Usually enzymes have the optimum pH between
6 and 8.
Q. Are there any important exceptions for this gen-
eral rule? (Page 39)
A. Pepsin (optimum pH 1-2), alkaline phosphatase
(optimum pH 9-10) and Acid phosphatase (4-5).
Q. What is zymogen? (Page 39)
A. It is otherwise called pro-enzyme. Inactive zy-
mogen is activated by removal of a piece of the
pro-enzyme.
Q. Give an example of zymogen is activated?
(Page 39)
A. By splitting a single peptide bond, and removal
of a small polypeptide from trypsinogen, the ac-
tive trypsin is formed. This results in unmasking
of the active centre.
Enzymology-I 35
Q. What is the significance of zymogen activation?

(Page 39)
A. Gastro-intestinal enzymes are synthesised in the
form of pro-enzymes, and only after secretion into
the alimentary canal, they are activated. This pre-
vents autolysis of cellular structural proteins. Co-
agulation factors are seen in blood as zymogen
form, their activation takes place only when ne-
cessity arises. This prevents intravascular coagu-
lation.
Q. What are the different types of inhibitions of
enzyme activity? (Page 39)
A. Competitive inhibition, non-competitive inhibi-
tion, suicide inhibition, and allosteric regulation.
Q. What are salient features of competitive inhibi-
tion? (Page 40)
A. Competitive inhibitor is a structural analogue. 2.
It is reversible. 3. Km is increased. 4. Vmax is not
changed.
Q. Give examples of competitive inhibition.
(Page 40)
A. Malonate inhibits succinate dehydrogenase.
Q. Give examples of clinical application of competi-
tive inhibition. (Page 40)
A. Sulfonamide inhibits PABA incorporation in bac-
teria, and so acts as an antibacterial agent. Meth-
otrexate inhibits folate reductase system,
dicoumarol inhibits vitamin K.
Q. What is the immediate treatment for methanol

poisoning? (Page 41)
A. Methanol is oxidised by alcohol dehydrogenase
to formaldehyde which causes the acute toxicity.
Antidote to methanol poisoning is ethanol which
is the natural substrate for alcohol dehydrogenase.
So ethanol is preferentially utilised.
Q. What are the salient features of non-competitive
inhibition? (Page 41)
A. Non-competitive inhibitor has no structural simi-
larity with the substrate. 2. It is generally not re-
versible 3. Km is not changed. 4. Vmax is reduced.
Q. Give examples of non-competitive inhibition.
(Page 41)
A. Di-isopropyl fluoro phosphate inhibits trypsin,
fluoride inhibits and enolase.
Q. Iodo-acetate inhibits enzyme by reacting with
which group at the active site of the enzyme?
(Page 41)
A. Sulfhydryl group.
Q. What is the mechanism of inhibitory action of
Di-isopropyl fluoro phosphate? (Page 41)
A. It inhibits enzymes with serine in their active cen-
tres, e.g. acetylcholine esterase.
Q. What is suicide inhibition? (Page 42)
A. In suicide inhibition, the structural analogue is
converted to a more effective inhibitor with the
help of the enzyme to be inhibited. The inhibitor
makes use of the enzyme’s own reaction mecha-
nism to inactivate it.
Enzymology-I 37
Q. What is the other term for suicide inhibition?

(Page 42)
A. Mechanism based inactivation.
Q. Give examples for suicide inhibition. (Page 42)
A. Ornithine decarboxylase (ODC) is inhibited by
difluro methyl ornithine (DFMO). Another ex-
ample is Allopurinol which is oxidised by xan-
thine oxidase to alloxanthine that is a strong in-
hibitor of xanthine oxidase.
Q. What is allosteric inhibition? (Page 42)
A. Allosteric enzyme has one catalytic site where the
substrate binds and another separate allosteric
site where the modifier binds.
Q. What are the salient features of allosteric inhibi-
tion? (Page 43)
A. (1) The inhibitor is not a substrate analogue. (2) It
is partially reversible when excess substrate is
added. (3) Km is usually increased. (4) Vmax is
reduced. (5) Most allosteric enzymes possess qua-
ternary structure. They are made up of subunits.
Q. Give examples for allosteric inhibition.
(Table 5.7)
A. ALA synthase, aspartyl trans-carbamoylase,
HMG CoA reductase
Q. What is covalent modification? (Page 43)
A. It means, either addition of a group to the enzyme
protein by a covalent bond; or removal of a group
by cleaving a covalent bond.
Q. Give some examples of covalent modification.

(Page 44)
A. Glycogen synthase is inactive, in the phosphory-
lated state, whereas glycogen phosphorylase is
active when phosphorylated.
Q. What is meant by induction? (Page 44)
A. Induction is effected at the level of DNA. The in-
ducer will relieve the repression on the operator
site and will remove the block on the biosynthe-
sis of the enzyme molecules.
Q. Give an example of induction. (Page 44)
A. Induction of lactose-utilising enzymes in the bac-
teria when the media contains lactose in the ab-
sence of glucose. In humans, Tryptophan
pyrrolase and transaminases are induced by glu-
cocorticoids. Glucokinase is induced by glucose.
ALA synthase is induced by barbiturates.
Q. What are constitutive enzymes? (Page 44)
A. Enzymes whose concentration in a cell is inde-
pendent of inducer are called constitutive en-
zymes.
Q. What is repression? (Page 44)
A. Repression acts at the gene level, the number of
enzyme molecules is reduced in the presence of
repressor molecule.
Q. Give an example of repression. (Page 44)
A. The key enzyme of heme synthesis, ALA synthase
is autoregulated by the heme by means of repres-
sion.
Enzymology-I 39
Q. Give examples of multi-enzyme complexes.

(Page 44)
A. Fatty acid synthase, pyruvate dehydrogenase, and
alpha keto glutarate dehydrogenase.
Q. What are the types of specificity shown by en-
zymes? (Page 45)
A. Absolute specificity, group specificity and
streospecificity.
Q. Give an example for absolute specificity.
(Page 45)
A. Urea is the only substrate for urease.
Q. Give an example for group specificity. (Page 45)
A. trypsin can hydrolyse peptide bonds formed by
carboxyl groups of arginine or lysine residues.
Enzymology-II
Iso-Enzymes and
Clinical Enzymology
Q. What are iso-enzymes? (Page 46)

A. They are physically distinct forms of the same
enzyme activity. They have identical catalytic
properties, but differ in structure.
Q. How to differentiate iso-enzymes. (Page 46)
A. Electrophoresis, heat stability, km value, inhibi-
tor specificity, and tissue localization.
Q. Which is a functional enzyme in plasma?
(Page 46)
A. They are actively secreted into plasma, and have
some functions in the blood. For example, en-
zymes of blood coagulation.
Q. What is non-functional enzymes in plasma?
(Page 46)
A. They are coming out from cells due to normal
wear and tear.
Enzymology-II 41
Q. What is their clinical significance? (Page 46)

A. Their normal levels in blood are very low, but
are drastically increased during cell death (necro-
sis) or disease. Therefore, assays of these enzymes
are very useful in diagnosis of diseases.
Q. Lactate dehydrogenase has how many polypep-
tide subunits? (Page 47)
A. Four. It is a tetramer.
Q. Lactate dehydrogenase has how many iso-en-
zymes? (Page 47)
A. Five
Q. What are they? (Page 47)
A. H4, H3M, H2M2, M3H and M4 varieties, forming
five iso-enzymes. All these five forms are seen in
all persons.
Q. How do you separate LDH iso-enzymes in labo-
ratory? (Page 47)
A. By cellulose acetate electrophoresis at pH 8.6.
Q. LDH level in blood is increased in which condi-
tions? (Page 47)
A. Myocardial infarction, hemolytic anemias, mus-
cular dystrophy, carcinomas, leukemias, and any
condition which causes necrosis of body cells.
Q. How do you further investigate for myocardial
infarction? (Page 47)
A. LDH-1 (H4) iso-enzyme is increased.
Q. What is flipped pattern? (Page 47)

A. Normally LDH-2 (H3M1) concentration in blood
is greater than LDH-1 (H4), but this pattern is re-
versed in myocardial infarction, this is called
flipped pattern.
Q. What are the serum enzymes helpful in the di-
agnosis of myocardial infarction?
A. Lactate dehydrogenase (LDH) H4 iso-enzyme,
creatine kinase (CK) CK MB iso-enzyme and as-
partyl transaminase (AST).
Q. Creatine kinase (CK) level in serum is increased
in which conditions?
A. Myocardial infarction, muscular dystrophies.
(Page 48)
Q. What is the advantage of CK estimation over
LDH estimation to identify myocardial infarc-
tion? (Page 48)
A. The CK level starts to rise within three hours of
infarction. Therefore, CK estimation is very use-
ful to detect early cases, where ECG changes may
be ambiguous. The CK level is not increased in
hemolysis or in congestive cardiac failure; and
therefore CK has an advantage over LDH.
Q. What are the iso-enzymes of CK? (Page 48)
A. CK is a dimer, the subunits are called B for brain
and M for muscle. Therefore, three iso-enzymes
are possible.
Enzymology-II 43
Q. What are the origins of the CK iso-enzymes?

(Page 48)
A. Eighty percent of molecules in circulation are MM
(CK3) variety of skeletal origin, five percent in
circulation are MB (CK2) from heart, one percent
from brain (BB or CK1) and fifteen percent CKmt
from mitochondria.
Q. When do you estimate total CK and the iso-en-
zyme? (Page 48)
A. Estimation of total CK is employed in muscular
dystrophies and CK-MB iso-enzyme is estimated
to identify myocardial infarction.
Q. What is the advantage of cardiac troponin I over
other parameters to identify the myocardial inf-
arction? (Page 48)
A. Cardiac Troponin I is released into the blood
within four hours after the onset of cardiac symp-
toms, peaks at 12-16 hours and remains elevated
for 5-9 days post-infarction. Therefore, CTI is very
useful as a marker at any time interval after the
heart attack. It is 75% sensitive index for myocar-
dial infarction.
Q. What is the significance of AST? (Page 48)
A. It is significantly elevated in myocardial infarc-
tion and moderately elevated in liver diseases.
Q. What is the significance of ALT? (Page 49)
A. Very high values are seen in acute hepatitis. Rise
in ALT levels may be noticed several days before
clinical signs such as jaundice are manifested.
Moderate increase may be seen in chronic liver
diseases such as cirrhosis, and malignancy in liver.
Q. Alkaline phosphatase level in serum is elevated

in which conditions? (Page 49)
A. Moderate increase is seen in hepatic diseases (in-
fective hepatitis, alcoholic hepatitis). High levels
may be noticed in obstructive jaundice or
cholestasis. Very high levels are seen in bone dis-
eases such as Paget’s disease, rickets, osteomala-
cia, osteoblastoma, metastatic carcinoma of bone.
Q. For alkaline phosphatase, how many iso-en-
zymes are present? (Page 49)
A. Six.
Q. What is Regan iso-enzyme? (Page 49)
A. It is the iso-enzyme of alkaline phosphatase, in-
hibited by phenylalanine. It is of placental origin.
It is elevated in about 15% cases of carcinoma of
lung, liver and gut and then named as Regan iso-
enzyme or carcinoplacental iso-enzyme.
Q. It is said that nucleotide phosphatase (NTP) is a
better index of obstructive liver disease than al-
kaline phosphatase (ALP), why? (Page 49)
A. ALP level is increased in both liver and bone dis-
eases, but NTP is only in liver diseases.
Q. Estimation of gamma glutamyl transferase is use-
ful to detect which condition? (Page 50)
A. Alcohol abuse.
Q. What are the enzymes useful in diagnosing liver
pathology? (Page 50)
A. ALT, ALP, GGT, NTP.
Enzymology-II 45
Q. Give the clinical implications of these enzymes.

(Page 50)
A. In infective hepatitis, ALT level is increased; in
alcohol abuse, GGT level is increased; in obstruc-
tive jaundice, ALP level is increased.
Q. Serum acid phosphatase level is increased in
which condition? (Page 50)
A. Prostate carcinoma.
Q. Total acid phosphatase may increase in some
other conditions also; what are they? (Page 50)
A. Prostate carcinoma, secondary metastasis in
bones, per rectal examination, intravascular
hemolysis.
Q. In such conditions, iso-enzyme study is helpful
or not? (Page 50)
A. Yes, tartarate labile iso-enzyme is specific for pros-
tate carcinoma.
Q. What is the advantage of prostate specific anti-
gen? (Page 50)
A. PSA is very specific for prostate carcinoma.
Q. What are the enzymes useful as tumour mark-
ers? (Page 50)
A. Regan iso-enzyme of ALP for lung tumour;
tartarate labile iso-enzyme of ACP and Prostate
specific antigen (PSA) for prostate carcinoma;
Neuron specific enolase (NSE) for cancers of
neuro-endocrine origin.
Q. Pseudo-cholinesterase deficiency is manifested

as what? (Page 50)
A. Succinyl choline apnoea; prolonged apnea when
succinyl choline is given as anesthetic drug.
Q. Which enzyme deficiency is inherited as X-
linked? (Page 50)
A. Glucose-6-phosphate-dehydrogenase.
Q. How the deficiency of GPD is manifested?
(Page 51)
A. Drug induced hemolytic anemia.
Q. Acute pancreatitis can be diagnosed by estimat-
ing which enzymes? (Page 51)
A. Amylase and lipase.
Q. Name some enzymes that are used as therapeu-
tic agents. (Page 52)
A. Asparaginase for leukemia, streptokinase to dis-
solve clots, and pepsin for indigestion.
Methods of Separation & Purification of Biological
Compounds, Methods of Study of Metabolism 47
Methods of Separation
and Purification of
Biological Compounds,
Methods of Study of
Metabolism
Q. What is meant by electrophoresis? (Page 53)

A. The term refers to the movement of charged par-
ticles through an electrolyte when subjected to an
electric field.
Q. What are the factors affecting the mobility in elec-
trophoresis? (Page 53)
A. Net charge on the particles (pI of proteins), mass
and shape of the particles, the pH of the medium,
strength of electrical field, and properties of the
supporting medium.
Q. What are the types of electrophoresis? (Page 53)
A. Horizontal and vertical types.
Q. What are the supporting media used? (Page 53)
A. Filter paper, cellulose acetate, agar gel, agarose
gel, starch gel and polyacrylamide gel.
Q. Electrophoresis is commonly employed for what

purpose in laboratory?
A. For serum electrophoresis and to see abnormali-
ties in serum protein concentrations.
Q. What is the advantage of polyacrylamide gel?
(Page 53)
A. It has a molecular sieving effect and so separa-
tion is very efficient.
Q. What is immuno-electrophoresis? (Page 54)
A. Here electrophoretic separation is followed by an
antigen-antibody reaction.
Q. What is the principle of adsorption chromatog-
raphy? (Page 54)
A. separation is based on differences in adsorption
at the surface of a solid stationary medium.
Q. What is the principle of partition chromatogra-
phy? (Page 55)
A. the components of the mixture to be separated
are partitioned between the two phases depend-
ing on the partition co-efficient (solubility) of the
particular substances.
Q. What are the common types of partition chroma-
tography? (Page 55)
A. Paper chromatography and thin layer chromatog-
raphy.
Q. What is the advantage of TLC over paper chro-
matography? (Page 55)
A. TLC needs lesser time, and separation is more ef-
fective.
Q. What is Rf value? (Page 56)

A. It is the ratio of the distance travelled by the sub-
stance (solute) to the distance travelled by the sol-
vent. The Rf value is a constant for a particular
solvent system at a given temperature.
Q. What is the basic principle of ion-exchange chro-
matography? (Page 56)
A. Here, the separation is based on electrostatic at-
traction between charged molecules to oppositely
charged groups on the ion exchange resins.
Q. What is the principle of gel filtration chromatog-
raphy? (Page 56)
A. The separation is effected on the basis of the size
of the molecules. It is otherwise called molecular
sieving.
Q. Give the principle of affinity chromatography.
(Page 56)
A. The technique is based on the high affinity of spe-
cific proteins for specific chemical groups.
Q. Give an example of affinity chromatography.
(Page 57)
A. Separation and quantitation of glycated hemoglo-
bin.
Q. What is the quickest method for separation of
proteins? (Page 58)
A. HPLC.
Q. What is the principle of ultracentrifugation?

(Page 58)
A. Large molecules can be sedimented at high cen-
trifugal forces whereas small molecules cannot.
Rate of sedimentation depends on the size, shape
and density of solute particles.
Q. What is Svedberg unit? (Page 57)
A. Sedimentation constant is expressed in Svedberg
(S) units.
Q. What are the uses of ultracentrifugation?
A. 1. Separation of subcellular organelles. 2. Separa-
tion of lipoproteins. 3. Determination of molecu-
lar weight of proteins.
Q. What are the methods used to determine the
molecular weight of proteins?
A. (1) Ultracentrifugation, (2) Gel filtration and (c)
PAGE (poly acrylamide gel electrophoresis).
(Page 57)
Q. What is the advantage of radio-immuno assay?
(Page 57)
A. Very small quantities of substances could be ac-
curately measured.
Q. What is the radio-active label used for RIA?
(Page 58)
A. Iodine-125.
Q. What is the half life of Iodine-125? (Page 58)
A. About 60 days.
Q. What are the disadvantages of RIA, when com-

pared to ELISA? (Page 58)
A. 1. Since radio-isotopes are used, only approved
laboratories could take up the assay. 2. The shelf
life of the reagent is short.
Q. What are the enzymes commonly used in ELISA
technique. (Page 58)
A. Alkaline phosphatase (ALP) and horse radish per-
oxidase (HRP).
Carbohydrates-I:
Chemistry, Digestion
and Absorption
Q. How carbohydrates are classified? (Page 61)

A. Based on the number of the sugar units available,
they are classified as monosaccharides, disaccha-
rides, oligosaccharides, and polysaccharides.
Q. What is a monosaccharide? (Page 61)
A. Molecules having only one actual or potential
sugar group are called monosaccharides.
Q. What is a polysaccharide? (Page 61)
A. They contain more than 10 sugar units.
Q. How are they combined together? (Page 61)
A. Through glycosidic linkages.
Q. How are monosaccharides further classified?
(Page 61)
A. Sugars having aldehyde group are called aldoses
and sugars with keto group are ketoses.
Carbohydrates-I 53
Q. Name some important monosaccharides.

(Page 61)
A. Glucose, fructose, galactose, mannose.
Q. What are pentoses? (Page 61)
A. Monosaccharides with five carbon atoms.
Q. Name a few pentoses. (Page 61)
A. Arabinose, Xylose, Ribose.
Q. Which is the reference carbon atom in sugars?
(Page 62)
A. Penultimate carbon atom.
Q. What is the difference between D and L sugars?
(Page 62)
A. They are mirror images with reference to
penultimate carbon atom.
Q. Which isomer is common in nature? (Page 62)
A. D variety of sugars are common in nature.
Q. Which is the most common monosaccharide in
the body?
A. Glucose. (Page 62)
Q. What is the difference between glucose and ga-
lactose? (Page 62)
A. They are different with regard to the H and OH
groups at the 4th carbon atom. Galactose is the
4th epimer of glucose (Fig.8.3).
Q. Galactose is present in which food? (Page 62)
A. Lactose is present in milk. Lactose contains ga-
lactose and glucose.
Q. What is epimerism? (Page 62)

A. When sugars are different from one another, only
in configuration with regard to a single carbon
atom (other than the reference carbon atom), they
are called epimers.
Q. Give an example. (Page 62)
A. For example, glucose and mannose are an
epimeric pair which differ only with respect to
carbon atom 2. Similarly, galactose is the 4th
epimer of glucose. (Fig. 8.3).
Q. Anomerism is produced with reference with
which carbon atom? (Page 62)
A. Anomers are produced by the spatial configura-
tion with reference to the first carbon atom in al-
doses and second carbon atom in ketoses. (Fig.
8.4).
Q. How alpha and beta forms of sugars are pro-
duced? (Page 62)
A. These are anomers. The difference lies in the spa-
tial configuration with reference to the first car-
bon atom in aldoses and second carbon atom in
ketoses. (Fig. 8.4).
Q. What is the basis of mutarotation? (Page 62)
A. It is due to the anomeric carbon atom.
Q. What is the difference between glucose and fruc-
tose?
A. Glucose is an aldohexose, and fructose is a
ketohexose.
Carbohydrates-I 55
Q. Name a ketose. (Page 63)

A. Fructose.
Q. What is the principle of Benedict’s test?
(Page 64)
A. In alkaline medium, sugar will cause reduction
of cupric ions, to form red coloured precipitate.
Q. What is the composition of Benedict’s reagent.
(Page 64)
A. It contains sodium carbonate, copper sulfate and
sodium citrate. In the alkaline medium provided
by sodium carbonate, the copper remains as cu-
pric hydroxide. Sodium citrate acts as a stabilising
agent to prevent precipitation of cupric hydrox-
ide.
Q. Benedict’s test is commonly employed for what?
(Page 64)
A. To detect the presence of glucose in urine.
Q. Name a few reducing sugars. (Page 64)
A. Glucose, fructose, mannose.
Q. Keto group is non-reducing, but fructose reduces
Benedict’s solution, what is the cause for this
anomaly? (Fig. 8.10)
A. In alkaline medium, ketone group is converted
to aldehyde, through enediol formation.
Q. In the case of sugars, which of the properties go
hand in hand?
A. Reducing property, osazone formation and mu-
tarotation. (page 64)
Q. Glucose and fructose will form identical

osazones, why?
A. The difference in glucose and fructose is depen-
dent on the first and second carbon atoms, and
this is masked by the osazone formation.
(Page 64)
Q. On oxidation of glucose, what are produced?
(Page 64)
A. Glucuronic acid, gluconic acid and glucos-
accharic acid.
Q. Reduction of glucose produces what? (Page 64)
A. Sorbitol.
Q. Name some deoxy sugars. (Page 66)
A. Deoxy ribose, fucose (deoxy galactose).
Q. Which is the stain used to identify deoxysugar?
(Page 66)
A. Feulgen staining.
Q. Name some important disaccharides. (Page 67)
A. Sucrose, lactose, maltose.
Q. What is the glycosidic linkage in lactose?
(Page 67)
A. Beta 1-4 linkage.
Q. What is the glycosidic linkage in sucrose?
(Page 67)
A. 1-2 linkage.
Carbohydrates-I 57
Q. Which disaccharide has no free aldehyde or ke-

tone group?
A. Sucrose. (Page 67)
Q. Glucose and fructose are reducing sugars, but
sucrose (containing glucose and fructose) is a
non-reducing sugar, why? (Page 67)
A. Because the glycosidic linkage in sucrose involves
1st carbon of glucose and 2nd carbon of fructose,
so both reducing groups are masked.
Q. Hydrolysis of maltose will give rise to what ?
(Page 67)
A. Two glucose units.
Q. Which is the sugar found in milk? (Page 67)
A. Lactose.
Q. What are the component monosaccharides of lac-
tose? (Page 67)
A. Galactose and glucose.
Q. Sucrose consists of what monosaccharides?
(Page 67)
A. Glucose + fructose.
Q. Name reducing disaccharides. (Page 67)
A. Lactose and maltose.
Q. How polysaccharides are classified? (Page 68)
A. Homopolysaccharides (homoglycans) and
heteropolysaccharides (heteroglycans).
Q. What is a homopolysaccharide? (Page 68)
A. They are composed of single kind of monosac-
charides.
Q. Give examples of homopolysaccharides.

(Page 68)
A. Starch, and glycogen.
Q. What are heteropolysaccharides? (Page 68)
A. They are composed of two or more different
monosaccharides.
Q. What are the characteristics of glycogen?
(Page 69)
A. It is composed of glucose units. It is the stored
form of carbohydrate in animal kingdom. It has a
highly branched structure.
Q. What is the reserve carbohydrate in plant king-
dom? (Page 69)
A. Starch.
Q. What is the end product of action of pancreatic
amylase on starch? (Page 69)
A. Maltose.
Q. Cellulose and starch are polysaccharides made
of glucose, but cellulose cannot be digest by
human beings, why? (Page 69)
A. Cellulose contains beta 1,4 linkages, which can-
not be digested by human enzymes.
Q. What is inulin? (Page 69)
A. It is a homopolysaccharide, composed of fructose
units.
Q. What is the use of inulin? (Page 69)
A. It is used to find renal clearance and glomerular
filtration rate.
Carbohydrates-I 59
Q. Give examples of heteropolysaccharides.

(Page 70)
A. Agar, hyaluronic acid, heparin, chondroitin sul-
fate.
Q. What are mucopolysaccharides? (Page 70)
A. They contain uronic acid and amino sugars.
Q. Which heteropolysaccharide does not contain
uronic acid? (Page 70)
A. Keratan sulfate.
Q. Hyaluronic acid is seen in which tissues?
(Page 70)
A. Connective tissue, synovial fluid, tendons, vitre-
ous humor.
Q. What is the difference between glycoprotein and
mucoprotein? (Page 71)
A. If the carbohydrate content is less than 10%, it is
called a glycoprotein. If the carbohydrate content
is more than 10% it is a mucoprotein.
Q. The rate of absorption of sugars in intestine is
highest for which monosaccharide? (Page 71)
A. Absorption rate of galactose is more than glucose,
while fructose is absorbed at a lesser rate than
glucose.
Q. Glucose is absorbed at the luminal side of gastro
intestinal cells by which mechanism?
(Page 72, and Fig. 8.30)
A. Carrier mediated co-transport with sodium,
named as sodium dependent glucose transporter
(SGluT).
Q. How glucose is released from intestinal cells into

the blood stream?
A. Glucose transporter type 2 (GluT2) (Fig.8.30).
Q. How glucose is taken up by cells from blood
stream? (Page 72)
A. In tissues GluT2 is involved in absorption of glu-
cose from blood.
Q. What is the importance of GluT4? (Page 72)
A. It is the glucose transporter present in muscle and
adipose tissues. Insulin induces these transport-
ers. In diabetes mellitus, entry of glucose into
muscle is decreased, because GluT4 is reduced
in insulin deficiency.
Q. What is the glucose sensor in the beta cells of
pancreas? (Page 72)
A. GluT2 acts as the glucose sensor mechanism, for
the controlled supply of insulin into blood stream.
Carbohydrates-II 61
Carbohydrates-II:
Major Metabolic
Pathways of Glucose,
Glycolysis, Gluconeogenesis,
Glycogen Metabolism
Q. What is glycolysis? (Page 73)

A. In this pathway, glucose is converted to pyruvate
or lactate, along with production of a small quan-
tity of energy.
Q. In which condition pyruvate is produced, and
when lactate? (Page 73)
A. In aerobic condition pyruvate is produced. When
oxygen is lacking, lactate is produced.
Q. What is the significance of Glycolysis?(Page 73)
A. It is the only pathway that is taking place in all
the cells of the body. Glycolysis is the only source
of energy in erythrocytes. Moreover, anaerobic
glycolysis forms the major source of energy in
actively contracting muscles.
Q. What is hexokinase? (Page 73)

A. Hexokinase is the first step in the glycolysis path-
way. It phosphorylates glucose to glucose-6-phos-
phate.
Q. What is glucokinase? (Page 73)
A. The reaction is similar to hexokinase. But glucoki-
nase is present only in liver, acts specifically on
glucose, and is active when glucose level in blood
is increased after a food.
Q. Which tissues prefer anaerobic glycolysis?
(Page 73)
A. RBCs, exercising muscle, and cancer cells.
Q. What is the importance of phospho fructokinase?
(Page 74)
A. It is the key enzyme (rate limiting enzyme) of the
pathway. It is an irreversible reaction.
Q. What is the substrate for aldolase reaction?
(Page 74)
A. Fructose-1,6-bisphosphate.
Q. During glycolysis, energy is produced during
which steps? (Page 74, 75)
A. Step 5, glyceraldehyde-3-phosphate to 1,3-
bisphospho glycerate, Step 6, 1,3-bis phospho
glycerate to 3-phospho glycerate, and Step 9,
Phospho enol pyruvate to pyruvate.
Q. Fluoride ions inhibit which enzyme? (Page 75)
A. Enolase.
Carbohydrates-II 63
Q. What is the importance of the above inhibition?

(Page 75)
A. Fluoride is used to prevent glycolysis, as preser-
vative for blood before glucose estimation.
Q. NAD is reduced to NADH in which reaction of

glycolysis? (Page 75)
A. Glyceraldehyde-3-phosphate dehydrogenase re-
action.
Q. NADH is oxidised to NAD in which reaction of
glycolysis? (Page 76)
A. Lactate dehydrogenase reaction.
Q. What are substrate level phosphorylations in gly-

colysis? (Page 75, 76)
A. 1,3-bisphospho glycerate kinase (step 6) and pyru-
vate kinase (step 9).
Q. What is the purpose of lactic acid production
under anaerobic conditions?
A. NADH generated in the 5th step has to be
oxidised to NAD+. This can be done by oxygen.
But when oxygen is lacking, the 5th step has to be
coupled with the 10th step for regeneration of
NAD.
(See Fig. 9.11)
Q. As the end product of glycolysis, pyruvate and
NADH are formed. During anaerobiasis, this
NADH is reconverted to NAD+ by what mecha-
nism? (Page 76)
A. Lactate dehydrogenase reaction.
Q. As the end product of glycolysis, pyruvate and

NADH are formed. During aerobic conditions,
this NADH is reconverted to NAD+ by what
mechanism? (Page 76)
A. Oxygen.
Q. What is Cori’s cycle? (Fig.9.13)
A. During exercise, lactate is produced in muscle.
This lactate diffuses into the blood. Lactate then
reaches liver, where it is oxidised to pyruvate. It
is then taken up through gluconeogenesis path-
way, and becomes glucose. This glucose can en-
ter into blood and then taken to muscle. This cycle
is called Cori’s cycle, or lactic acid cycle.
Q. What is the purpose of Cori’s cycle? (Page 77)
A. By this means, the lactate is efficiently reutilised
by the body.
Q. Why lactate is transported from muscle to liver?
(Page 77)
A. Oxygen is limited in muscle, so lactic acid could
not be made to pyruvate in muscle. So, it is trans-
ported to liver, where it is made to pyruvate and
then to glucose.
Q. What are the inhibitors of phosphofructokinase?
(Page 77)
A. ATP, Citrate, Glucocorticoids.
Q. What are the activators of phospho fructo kinase?
(Page 77, 78)
A. AMP, Fructose-2,6-bisphosphate, Fructose-6-
phosphate.
Carbohydrates-II 65
Q. What are key glycolytic enzymes? (Page 77, 78)

A. Glucokinase, Phospho fructo kinase, Pyruvate ki-
nase.
Q. What is the action of insulin on glycolysis?
(Page 77, 78)
A. Insulin stimulates glycolysis.
Q. What is the net yield of ATP from one glucose
molecule during anaerobic glycolysis?
(Page 78 and Table 9.3)
A. 2 ATP.
Q. In aerobic glycolysis, the net yield from one glu-
cose molecule is how much?
A. 8 ATP.
Q. During complete oxidation, what is the net yield
of ATP from one glucose molecule?
A. 38 ATP.
Q. How many ATPs are generated per one rotation
of the citric acid cycle?
A. 12 ATP.
Q. What is the function of 2,3-bisphospho glycerate?
(Page 79)
A. When combined with hemoglobin, 2,3-BPG re-
duces the affinity towards oxygen.
Q. What are the steps in which carbon dioxide is
produced from a glucose molecule? (Page 80)
A. Pyruvate dehydrogenase, isocitrate dehydroge-
nase, alpha keto glutarate dehydrogenase.
Q. What are the co-enzymes necessary for oxidative

decarboxylation of pyruvate? (Page 80)
A. Thiamine pyrophosphate, NAD, FAD, Lipoic acid,
Co-enzyme A.
Q. What is pyruvate dehydrogenase? (Fig. 9.19)
A. The enzyme catalysing the reaction, pyruvate to
acetyl CoA.
Q. What is pyruvate carboxylase? (Fig. 9.20)
A. The enzyme catalysing the reaction, pyruvate to
oxaloacetate.
Q. What is pyruvate kinase? (Fig. 9.20)
A. It catalyses the reaction, phospho enol pyruvate
to pyruvate.
Q. There is no net synthesis of glucose from fatty
acids, why? (Page 80)
A. Pyruvate to acetyl CoA is a totally irreversible
reaction.
Q. Which enzyme irreversibly channels glucose to
energy production, rather than retaining glucose
for blood sugar regulation? (Page 80)
A. Pyruvate dehydrogenase is an irreversible reac-
tion.
Q. Pyruvate is converted to acetyl CoA by which
enzyme? (Page 80)
A. Pyruvate dehydrogenate.
Q. What is gluconeogenesis? (Page 81)
A. Production of glucose from non-carbohydrate
sources.
Carbohydrates-II 67
Q. What are those non-carbohydrate sources? (What

are the substrates for gluconeogenesis?).
(Page 82, 83)
A. Glucogenic amino acids and lactate.
Q. What are the key gluconeogenic enzymes?
(Page 82)
A. Pyruvate carboxylase, Phospho enol pyruvate
carboxy kinase, Fructose-1,6-bisphosphatase and
Glucose-6-phosphatase.
Q. Pyruvate carboxylase reaction (pyruvate to ox-
aloacetate) needs which co-enzyme? (Page 81)
A. Biotin and ATP.
Q. Malate shuttle is used for what purpose?
(Page 82)
A. Reactions of gluconeogenesis are taking place in
cytosol. Hence the oxaloacetate has to be trans-
ported from mitochondria to cytosol. This is
achieved by the malate shuttle (see Fig. 9.22).
Q. Gluconeogenesis is taking place in which tissue?
(Page 81)
A. Liver.
Q. How many ATP molecules are required to con-
vert two molecules of pyruvate into glucose?
(Page 82)
A. Six.
Q. Blood glucose level can be raised by gluconeo-
genesis only by liver, why? (Page 82)
A. Glucose-6-phosphatase is present only in liver.
Q. Muscle glycogen will not serve as a precursor of

blood sugar, why? (Page 82)
A. Glucose-6-phosphatase is absent in muscle.
Q. Which amino acids are both ketogenic and gluco-
genic? (Fig. 9.29)
A. Tyrosine and tryptophan.
Q. What will inhibit gluconeogenesis? (Page 85)
A. Insulin.
Q. What will stimulate gluconeogenesis? (Page 85)
A. Glucagon and glucocorticoids.
Q. What is the significance of gluconeogenesis?
(Page 85)
A. Gluconeogenesis is necessary to maintain blood
glucose level especially under conditions of star-
vation.
Q. What is glycogenolysis? (Page 86)
A. Degradation of glycogen to glucose.
Q. What is the main enzyme for glycogenolysis?
(Page 86)
A. Glycogen phosphorylase.
Q. Which hormones enhance glycogenolysis?
(Page 87)
A. Adrenaline and glucagon causes glycogenolysis.
Q. What is the mechanism of action of adrenaline?
(Page 87)
A. Adrenaline increases cyclic AMP level which ac-
tivates glycogen phosphorylase.
Carbohydrates-II 69
Q. In the glycogen synthesis, which is the active

glucose derivative?
A. UDP-glucose.
Q. Adrenaline acts on which enzyme?
A. Glycogen phosphorylase.
Q. What will activate glycogen phosphorylase?
(Page 87)
A. Epinephrine, glucagon, cyclic AMP.
Q. Which is the defective enzyme in von Gierke’s
disease (glycogen storage disease type I)?
(Page 89)
A. Glucose-6-phosphatase.
Q. What are the characteristic clinical features of von
Gierke’s disease?
A. Fasting hypoglycemia, which does not respond
to adrenaline is very characteristic. (Page 89)
Carbohydrates-III:
Regulation of Blood Sugar,
Insulin and Diabets Mellitus
Q. What is the level of fasting blood sugar in a nor-

mal person?
A. 70-110 mg/dl. (Page 90)
Q. Which hormone is hypoglycemic? (Page 90)
A. Insulin.
Q. What are the major actions of insulin? (Page 90)
A. Insulin decreases blood sugar, it stimulates gly-
colysis, inhibits gluconeogenesis, enhances glyco-
gen synthesis and inhibits lipolysis.
Q. What are the anti-insulin (hyperglycemic) hor-
mones? (Page 90)
A. Glucagon, adrenaline, corticosteroids, growth
hormone.
Q. What are the major actions of glucagon?
(Page 91)
A. Promotes glycogenolysis, enhances gluconeogen-
esis, depresses glycogen synthesis, inhibits gly-
colysis.
Carbohydrates-III 71
Q. What is the best method for glucose estimation?

(Page 91)
A. Glucose oxidase peroxidase (GOD-POD) method.
Q. What is the major indication for doing an oral
glucose tolerance test (OGTT)? (Page 92)
A. Patient has symptoms suggestive of diabetes mel-
litus, but fasting blood sugar value is inconclu-
sive (between 100 and 126 mg/dl).
Q. What are the precautions to take before OGTT?
(Page 92)
A. Patient should have a good carbohydrate diet for
three days prior to the test. Patient should avoid
insulin and oral antidiabetic drugs. Patient should
fast overnight. Patient should not take any break-
fast.
Q. What is the glucose load dose? (Page 92)
A. Seventy five gram anhydrous glucose (82.5 g of
glucose monohydrate) in 250-300 ml of water.
Q. What precaution would you take in giving the
glucose load? (Page 92)
A. In order to prevent vomiting, patient is asked to
drink it slowly (within about 5 minutes).
Flavouring of the solution will also reduce the
tendency to vomit.
Q. What are the criteria for diagnosing diabetic
mellitus? (Table 10.1). (Page 92)
A. Fasting plasma sugar is more than 126 mg/dl, on
more than one occasion. 2. Or, if 2-hour post-glu-
cose load value of OGTT is more than 200 mg/dl
(even at one occasion). 3. Or, if both fasting and 2-
hour values are above these levels, on the same
occasion.
Q. Can you diagnose diabetes on the basis of ran-

dom blood estimations? (Page 92)
A. Diabetes is diagnosed, if the random plasma sugar
level is more than 200 mg/dl, on more than one
occasion. Diagnosis should not be based on a
single random test alone, it should be repeated.
Q. When a standard oral glucose tolerance test was
done, the blood glucose levels of the patient were
found as:0 min = 130 mg/dl and 120 min = 220 mg
/dl. What will be your diagnosis? (Page 92)
A. Diabetes mellitus.
Q. What is impaired glucose tolerance (IGT)?
(Page 93)
A. When fasting plasma glucose level is between 110
and 126 mg/dl and 2-hour post-glucose value is
between 140 and 200 mg/dl.
Q. When a standard oral glucose tolerance test was
done, the blood glucose levels of the patient were
found as:0 min = 120 mg/dl, 120 min = 160 mg /
dl. What is your diagnosis?
A. Impaired glucose tolerance. (Page 93)
Q. What you will do for such persons? (Page 93)
A. Such persons need careful follow up because IGT
progresses to frank diabetes at the rate of 2% pa-
tients per year.
Q. What is impaired fasting glycemia (IFG).
(Page 93)
A. In this condition, fasting plasma sugar is abnor-
mal (between 110 and 126 mg/dl), but the 2-hour
post-glucose value is within normal limits (less
than 140 mg/dl).
Q. What you will do for such persons? (Page 93)

A. These persons need no immediate treatment, but
are to be kept under constant check-up. They are
at increased risk for development of diabetes or
cardiovascular diseases.
Q. What is gestational diabetes mellitus (GDM)?
(Page 93)
A. This term is used when carbohydrate intolerance
is noticed, for the first time, during a pregnancy.
If the fasting value is more than 126 mg%, it is
taken as gestational diabetes.
Q. If a known diabetic patient, who becomes preg-
nant, will you include her in the category of
GDM? (Page 93)
A. No.
Q. What is the clinical significance of GDM?
(Page 93)
A. Women with GDM are at increased risk for sub-
sequent development of frank diabetes. GDM is
associated with increased birth weight of child
and increased incidence of neonatal mortality.
Q. After delivery, what you will do for a person with
GDM? (Page 93)
A. After the child birth, the women should be re as-
sessed and accordingly classified as having either
diabetes mellitus or normal glucose tolerance,
based on the results of a fresh OGTT.
Q. What are other conditions which may cause im-
paired glucose tolerance? (Page 93)
A. Alimentary glucosuria, renal glucosuria.
Q. What is renal glucosuria? (Page 93)

A. Here glucose is excreted in urine due to a lower-
ing of renal threshold. The blood sugar levels are
within normal limits.
Q. What is normal renal threshold for glucose?
(Page 93)
A. 180 mg/100 ml.
Q. What are the reducing substances seen in urine?
(Page 94)
A. Glucose, fructose, lactose, galactose, pentoses,
ascorbic acid, glucuronides.
Q. What is transient glucosuria? (Page 94)
A. It may occur in some people due to emotional
stress. Excessive secretion of catecholamines will
produce hyperglycemia and resultant glucosuria.
Once theÿstress is removed, the glucosuria dis-
appears.
Q. What is fructosuria? (Page 94)
A. Presence of fructose in urine. It is due to the defi-
ciency of fructokinase or aldolase B (Fig.11.11).
Q. What is lactosuria? (Page 94)
A. It is observed in the urine of normal women dur-
ing 3rd trimester of pregnancy and during lacta-
tion.
Q. What is the clinical importance of lactosuria?
(Page 94)
A. The condition is harmless. But it is important to
distinguish lactosuria from glucosuria when ges-
tational diabetes mellitus is suspected.
Q. What is the test for reducing sugars in urine?

(Page 95)
A. Benedict’s test.
Q. What are the pathways stimulated by insulin?
(Page 96)
A. Glycolysis, glycogen synthesis, HMP shunt path-
way, lipogenesis.
Q. Name important enzymes that are stimulated by
Insulin. (Page 96)
A. Phospho fructo kinase, glycogen synthase, glu-
cose-6-phosphate dehydrogenase, acetyl CoA car-
boxylase.
Q. What are the pathways inhibited by insulin?
(Page 96)
A. Gluconeogenesis, glycogenolysis, lipolysis, keto-
genesis.
Q. What are the important enzymes inhibited by
insulin? (Page 96)
A. Glucose-6-phosphatase, glycogen phosphorylase,
hormone sensitive lipase.
Q. Where is insulin synthesised? (Page 96)
A. Beta cells of langerhans of pancreas.
Q. What is proinsulin? (Page 96)
A. Insulin is synthesised as a large single polypep-
tide. Middle part of it is then removed, to form
the A and B chains of insulin.
Q. What is C peptide? (Page 96)
A. It is the part removed from proinsulin during the
maturation of insulin molecule.
Q. What is the clinical significance of C peptide?

(Page 96)
A. Sometimes measurement of endogenous insulin
may be difficult because of the presence of anti-
bodies against insulin in the circulation. Then
measurement of C-peptide is useful.
Q. What are the salient structural features of insu-
lin? (Page 96)
A. Insulin is a protein hormone with two poly peptide
chains, the A chain with 21 amino acids and the B
chain with 30 amino acids are joined together by a
pair of disulfide bonds. It has a total of 51 amino
acids.
Q. How is insulin secretion controlled? (Page 96)
A. Glucose is the major stimulant of insulin secre-
tion.
Q. How glucose stimulates insulin secretion?
(Page 96)
A. The beta cells have GluT 2 receptors, these act as
sensor mechanism for glucose level. The insulin
secretion is controlled by a cyclic AMP-mediated
mechanism. Cyclic AMP along with calcium
causes the insulin secretion.
Q. What is the effect of insulin on glucose uptake
of cells? (Page 97)
A. Insulin facilitates the membrane transport of glu-
cose in most of tissues, especially in muscles and
adipose tissue. This is by glucose transporter,
GIuT4. But glucose uptake by GlT2 is indepen-
dent of insulin, it is seen in liver and brain.
Q. Maximum glucose utilisation is seen in which

tissue? (Page 97)
A. At basal rates, brain utilises 60% of sugar oxidised.
Q. What is the mechanism of action of insulin?
(Page 97)
A. Insulin acts by binding to membrane receptor, on
the target cells.
Q. What is the structural feature of insulin recep-
tor? (Page 97)
A. Insulin receptor has four subunits, two alpha and
two beta subunits. The alpha units are located on
the extracellular side, to which insulin binds. The
beta subunits are towards cytoplasmic side. Beta
subunit has tyrosine kinase activity.
Q. How diabetes mellitus is classified? (Page 99)
A. Type 1 and type 2.
Q. What are the characteristic features of type 1, dia-
betes mellitus?
A. Here circulating insulin level is deficient. These
patients are dependent on insulin injections. On-
set is during adolescence. Rapid loss of body
weight is observed. They are more prone to de-
veloping ketosis.
Q. What about type 2 diabetes mellitus? (Page 100)
A. Most of the patients belong to this type. Here cir-
culating insulin level is normal, but there is a rela-
tive insulin deficiency. It is commonly seen in in-
dividuals above 40 years. These patients are less
prone to developing ketosis.
Q. What is maturity onset diabetes of young

(MODY)? (Page 100)
A. It is due to defective glucokinase.
Q. What are the cardinal symptoms of diabetes mel-
litus? (Page 100)
A. Polyuria, polydypsia, polyphagia and weight
loss.
Q. What is the reason for polyuria in diabetes mel-
litus? (Page 100)
A. When the blood glucose level exceeds the renal
threshold glucose is excreted in urine. Due to os-
motic effect, more water accompanies the glucose.
Q. What is the reason for polydypsia in diabetes
mellitus? (Page 100)
A. To compensate for this loss of water, thirst centre
is activated, and more water is taken (polydypsia).
Q. What is the reason for weight loss in diabetes
A. The loss and ineffective utilisation of glucose
leads to breakdown of fat and protein.ÿThis would
lead to loss of weight.
Q. What is the reason for polyphagia in diabetes
A. To compensate the loss of glucose and protein,
patient takes more food.
Q. What are the acute complications of diabetes
A. Keto acidosis, hyperosmolar non-ketotic coma,
lactic acidosis.
Q. What are the chronic complications of diabetes

A. Thrombosis, paralysis, gangrene, micro-angiopa-
thy, nephrosclerosis, cataract, peripheral neuropa-
thy.
Q. What is micro-albuminuria? (Page 101)
A. Albumin 50 to 300 mg/day in urine. It is a pre-
dictor of progressive renal damage, atheroscle-
rotic diseases and cardiovascular mortality. Al-
bumin more than 300 mg/day indicates overt dia-
betic nephropathy.
Q. What is the cause for cataract in diabetes melli-
tus? (Page 101)
A. Early development of cataract of lens is due to
the increased rate of sorbitol formation, caused
by the hyperglycemia.
Q. What is the difference between glycosylation
and glycation?
A. Enzymatic addition of any sugar to a protein is
called “glycosylation” while non-enzymatic pro-
cess is termed “glycation”. (Page 101)
Q. What is the basis of glycation? (Page 101)
A. When there is hyperglycemia, proteins in the body
may undergo glycation. It is a non-enzymatic pro-
cess. Glucose is added to the N-terminal amino
group of proteins.
Q. What is the significance of glycated hemoglobin?

(Page 101)
A. The determination of glycated hemoglobin is not
for diagnosis of diabetes mellitus, but for moni-
toring the response of treatment. It is unaffected
by recent food intake or recent changes in blood
sugar levels. An elevated glycohemoglobin indi-
cates poor control of diabetes mellitus. The risk
of retinopathy and renal complications are pro-
portionately increased with elevated glycatedhe-
moglobin.
Carbohydrates-IV 81
Carbohydrates-IV:
Other Metabolic Pathways
(HMP Shunt Pathway,
Fructose, Galactose,
Glucuronic Acid, Alcohol)
Q. HMP shunt pathway use how much glucose?

(Page 103)
A. About 10% of glucose molecules per day are en-
tering in this pathway.
Q. What are the tissues in which HMP shunt path-
way is significant? (Page 103)
A. Liver, adipose tissue, RBC, adrenal cortex, ovary,
testis, mammary gland, lens.
Q. Which is the key enzyme of hexose monophos-
phate shunt pathway? (Page 103)
A. Glucose-6-phosphate dehydrogenase.
Q. What is the hormonal control over HMP shunt
pathway? (Page 103)
A. Insulin stimulates the pathway by activating the
key enzyme.
Q. Which enzyme generates NADPH? (Page 103)

A. Glucose-6-phosphate dehydrogenase.
Q. What is the purpose of HMP shunt pathway?
(Page 104)
A. It generates NADPH.
Q. What is the use of NADPH in biological systems?
(Page 105)
A. For reductive biosynthesis.
Q. What reductive biosynthesis pathways need
NADPH? (Page 105)
A. Fatty acid biosynthesis, synthesis of cholesterol,
steroid hormones.
Q. Apart from reductive synthesis, NADPH is used
for what purpose? (Page 105)
A. It is necessary to keep the integrity of RBC mem-
brane, it is needed for keeping glutathione in re-
duced state, it is required for keeping transpar-
ency of lens, it is necessary for superoxide pro-
duction inside macrophages.
Q. What about ATP generation? NADPH is used for
that? (Page 106)
A. No. NADPH is not used for ATP generation.
Q. Apart from NADPH generation, is there any
other purpose for the HMPshunt pathway?
(Page 106)
A. The pathway is required for the synthesis of ri-
bose, the pentose phosphates are necessary for
nucleotide (DNA and RNA) synthesis.
Carbohydrates-IV 83
Q. What is the manifestation of glucose-6-phosphate

dehydrogenase deficiency? (Page 106)
A. Drug induced hemolysis and met-hemoglobinemia.
Q. Acute hemolytic episode after administration of
antimalarial drug is due to what? (Page 106)
A. Deficiency of glucose-6-phosphate dehydrogenase.
Q. What is the most common enzyme deficiency in
man? (Page 106)
A. Glucose-6-phosphate dehydrogenase deficiency.
Q. What is the mode of hereditary transmission of
GPD deficiency? (Page 106)
A. It is transmitted as an x-linked recessive character.
Q. Is there any advantage of the abnormal gene?
(Page 106)
A. The geographical distribution of GPD deficiency
correlates well with the malarial endemicity. The
GPD deficiency offers resistance to malarial in-
fection.
Q. What is the clinical significance of transketolase
enzyme? (Page 107)
A. The transketolase reaction is measured in RBCs
as an index of the thiamine status of an individual.
Q. Abnormal transketolase leads to what clinical
condition? (Page 107)
A. The occurrence of Wernick’s encephalopathy
(seen in alcoholics and in thiamine deficiency) is
due to a genetic defect in the enzyme transketo-
lase. It occurs owing to the enzyme having low
binding capacity for TPP.
Q. Transketolase activity is decreased in the defi-

ciency what? (Page 107)
A. Thiamine pyrophosphate (TPP).
Q. What is the purpose of uronic acid pathway?
(Page 107)
A. It is used for conjugation of bilirubin, steroids,
synthesis of gluco-saminoglycans.
Q. In lower animals, uronic acid pathway is used
for what purpose? (Page 107)
A. For synthesis of ascorbic acid (vitamin C).
Q. What is essential pentosuria? (Page 107)
A. Excretion of pentose (L-xylulose) in urine due to
the deficiency of xylitol dehydrogenase.
Q. What is its importance? (Page 107)
A. It does not produce any harm. But it gives a posi-
tive reaction to Benedict’s test, so it should be dif-
ferentiated from diabetes mellitus.
Q. What is the clinical significance of polyol path-
way? (Page 107)
A. The elevated level of sorbitol has been implicated
in the development of neuropathy, cataract and
retinopathy in diabetes mellitus.
Q. Fructokinase catalyses which reaction?
(Page 108)
A. Fructose to fructose-1-phosphate.
Q. What is fructose intolerance? (Page 108)
A. Due defective aldolase-B, fructose-1-phosphate
accumulates. This leads to accumulation of gly-
cogen in liver, and hypoglycemia.
Carbohydrates-IV 85
Q. Free fructose is seen in which body fluid?

(Page 108)
A. Seminal plasma.
Q. This fructose is produced by which pathway?
(Page 107)
A. Polyol pathway of glucose.
Q. What is the clinical application of fructose esti-
mation in semen? (Page 108)
A. Fructose is secreted by seminal vesicles. A block
in seminal vessels is indicated by the absence of
fructose in semen.
Q. What is fructosuria? (Page 108)
A. It is a benign metabolic defect due to deficiency
of fructokinase. Urine gives positive Benedict’s
test, and so it should be differentiated from dia-
betes mellitus.
Q. Neonatal hypoglycemia is seen in which condi-
tions? (Page 109)
A. Glycogen storage disease, type I, galactosemia,
fructose intolerance.
Q. What are the features of galactosemia?
(Page 109)
A. Congenital cataract, mental retardation, neonatal
hypoglycemia, hepatosplenomegaly, positive
Benedict’s test.
Q. Congenital cataract is seen in which condition?
(Page 109)
A. Galactosemia.
Q. Galactosemia is due the absence of which en-

zyme? (Page 109)
A. Galactose-1-phosphate uridyl transferase.
Q. What is the treatment policy in galactosemia?
(Page 110)
A. Lactose free diet is given for first five years of life.
Q. Why five years, why life-long treatment is not
required? (Page 110)
A. By five years, the alternate pathway (galatose-1-
phosphate pyrophosphorylase) becomes active.
Q. Why excessive intake of alcohol produces lactic
acidosis? (Page 110)
A. During alcohol oxidation, NADH is generated,
which converts pyruvate to lactate.
Q. Why excessive intake of alcohol produces hy-
poglycemia? (Page 110)
A. Because ethanol inhibits gluconeogenesis.
Q. What are the results of chronic alcoholism?
(Page 111)
A. Polyneuropathy, fatty liver, cirrhosis, Werneck’s
encephalopathy.
Q. How N-acetyl neuraminic acid (sialic acid) is
synthesised? (Page 111)
A. N-acetyl mannosamine-6-phosphate + phospho
enol pyruvate.
Carbohydrates-IV 87
Q. In glycoproteins, carbohydrate residues are at-

tached to which group of the polypeptide chain?
(Page 112)
A. Hydroxyl group of serine or threonine.
Q. Increased glucosaminoglycans in urine is seen
in which condition? (Page 113)
A. Mucopolysaccharidosis.
Lipids-I:
Chemistry, Digestion and
Absorption of Lipids
Q. How lipids are classified? (Page 115)

A. Simple, compound and derived.
Q. Classify fatty acids. (Page 115)
A. Depending on the total number of carbon atoms,
they are classified as even chain and odd chain.
Q. Which type is prevalent in human body?
(Page 115)
A. Even chain fatty acids.
Q. Fatty acids are classified in any other manner?
(Page 116)
A. They are also classified as saturated or unsatur-
ated fatty acids.
Q. What fatty acids are generally present in human
fat? (Page 116)
A. Mainly Oleic acid, then comes palmitic acid and
linoleic acid.
Lipids-I 89
Q. How many carbon atoms are present in oleic acid?

(Page 116)
A. 18 carbon, with one double bond.
Q. Name some unsaturated fatty acids. (Page 117)
A. Oleic, linoleic, linolenic and arachidonic acids.
Q. Name some polyunsaturated fatty acids.
(Page 117)
A. Linoleic, linolenic and arachidonic acids.
Q. What is the structure of linoleic acid?
(Page 117)
A. 18 carbon, with two double bonds.
Q. What is the structure of linolenic acid?
(Page 117)
A. 18 carbon with three double bonds.
Q. What is the structure of arachidonic acid?
(Page 117)
A. 20 carbon with four double bonds.
Q. Which contains good quantity of PUFA?

(Page 118)
A. Vegetable oils such as sunflower oil, ground nut
oil.
Q. Which contains very low level of PUFA?
(Page 118)
A. Coconut oil and animal fats.
Q. What is the advantage of storing energy as trig-

lycerides in the body? (Page 119)
A. Space requirement is less, storage does not require
water, can be mobilised whenever required, ca-
pacity for storage is unlimited.
Q. What is saponification? (Page 119)
A. Hydrolysis of fat by alkali is called are saponifi-
cation.
Q. Does saponification number of a fat molecule
increase or decrease with the molecular weight
of the fat? (Page 119)
A. Decreases with increase in molecular weight of
fat.
Q. Odour of rancid oil is due to what? (Page 119)
A. Partial oxidation of fatty acids, with formation of
epoxides and peroxides of small molecular
weight fatty acids.
Q. Complete digestion of triacyl glycerol (triglycer-
ide) in gastro intestinal tract needs what en-
zymes? (Page 120)
A. Pancreatic lipase, co-lipase, isomerase and bile
salts
Q. What is the function of pancreatic lipase?
(Page 120)
A. Partial hydrolysis of triacyl glycerol. The prod-
ucts are 2-mono acylglycerol (2-MAG) (?-mono-
glyceride) and two fatty acid molecule (Fig. 12.7).
Lipids-I 91
Q. What is the function of isomerase? (Page 120)

A. Isomerase shifts the ester bond from position 2 to
1, this is then hydrolysed by the lipase to form
free glycerol and fatty acid.
Q. Will there be complete breakdown of triglycer-
ide into fatty acid in the gastro intestinal tract?
(Page 120)
A. No, only partial digestion is possible.
Q. What are the final end products of digestion of
triglyceride? (Page 120)
A. 2-monoacyl glyceride (78%), 1-monoacyl glycer-
ide (6%), glycerol and fatty acids (14%).
Q. How small chain fatty acids are absorbed?
(Page 120)
A. Small chain and medium chain fatty acids (chain
length less than 14 carbons) are directly absorbed
from the intestinal lumen into the portal vein and
taken to the liver.
Q. How long chain fatty acids are absorbed?
(Page 120)
A. Long chain fatty acids (chain length more than 14
carbons) are absorbed by forming micelles with
the help of bile salts.
Q. How bile salts help in the absorption of dietary
lipids? (Page 120)
A. By emulsifying the lipids and producing micelles
of lipids.
Q. What is the chemical name of bile salts?
(Page 120)
A. Sodium glycocholate and sodium taurocholate.
Q. What are micelles? (Page 120)

A. The micelles are spherical particles with a hydro-
philic exterior and hydrophobic interior core (Fig.
12.8). Monoglycerides, long chain fatty acids, cho-
lesterol, phospholipids and lysophospholipids
are incorporated into molecular aggregates to
form mixed micelles.
Q. What happens to the micelles? (Page 120)
A. Fatty acids and monoacyl glycerides from the mi-
celles passively diffuse into the mucosal cell.
Q. What happens to the fatty acids in the mucosal
cell? (Page 120)
A. Once inside the intestinal mucosal cell, the long
chain fatty acids are re-esterified to form triglyc-
erides (Fig.12.9).
Q. What is the further fate of this triglyceride?
(Page 121)
A. The triglyceride, along with phospholipids,
apoproteins B48, and apo-A are incorporated into
chylomicrons. The chyle (milky fluid) from the
intestinal mucosal cells loaded with chylomicrons
are transported through the lacteals into the tho-
racic duct and then emptied into systemic circu-
lation.
Q. What is the difference for absorption of short
chain fatty acid? (Page 120)
A. Short and medium chain fatty acids do not need
re-esterification. They directly enter into blood
vessels (Not to lacteals).
Lipids-I 93
Q. Where will you find short and medium chain

fatty acids? (Page 120)
A. They are seen in butter, ghee, coconut oil and
mother’s milk.
Q. What happens to the bile salts of micelle?
(Page 120)
A. The bile salts are left behind.
Q. What is enterohepatic circulation of bile salts?
(Page 120)
A. They are separately reabsorbed from the ileum
and returned to the liver to be re-excreted again
to gut.
Q. What is steatorrhea? (Page 121)
A. When excretion of fat in faeces is more than 6 g
per day, it is called steatorrhea.
Q. What is it due to? (Page 121)
A. It is due to defective digestion as in chronic dis-
eases of pancreas. In such cases, unsplit fat is ex-
creted in feces.
Q. What happens in defective absorption?
(Page 121)
A. If the absorption alone is defective, most of the
fat in faeces may be split fat, i.e. fatty acids and
monoglycerides.
Q. What is the cause for defective absorption of fat?
(Page 121)
A. It may be due to diseases in intestinal mucosa,
e.g. coeliac disease, sprue, Crohn’s disease.
Q. Any other cause for defective absorption of fat?

(Page 121)
A. Any condition leading to a deficiency of bile salts
can also result in malabsorption of fat. The most
common causes are obstruction to biliary tract due
to gall stones, tumours of head of pancreas, en-
larged lymph glands, etc.
Q. What is the line of management in defective ab-
sorption? (Page 121)
A. In such cases, triglycerides with short chain and
medium chain fatty acids are digested and ab-
sorbed properly, because they do not require
micellerisation for absorption. Since milk fat and
coconut oil are made up of MCT, they are thera-
peutically useful in malabsorption syndromes.
Lipids-II 95
Lipids-II:
Metabolism of Fatty acids,
Fatty acid oxidation,
Fatty acid synthesis,
Lipolysis, Ketone bodies.
Q. How fatty acids are activated in preparation of

oxidation? (Page 122)
A. Fatty acids are activated to their co-enzyme A
(CoA) derivative.
Q. What is the enzyme for this activation?
(Page 122)
A. Thiokinase or fatty acyl CoA synthetase.
Q. How much ATP is required for this reaction?
(Page 122)
A. One molecule of ATP is hydrolysed to AMP and
PPI. Thus two high energy bonds are utilised in
this reaction.
Q. What are the co-enzymes needed for fatty acid
oxidation? (Page 122)
A. FAD and NAD.
Q. What is carnitine? (Page 122)

A. Carnitine is beta-hydroxy-gamma-trimethyl am-
monium butyrate. It is synthesised from lysine
and methionine in liver and kidney.
Q. What is the function of carnitine? (Page 122)
A. Fatty acids are activated in the cytoplasm, but the
beta-oxidation is in mitochondria. The long chain
fatty acyl CoA cannot pass through the inner mi-
tochondrial membrane. Therefore a transporter,
carnitine is involved in transfer of fatty acids.
Q. What about medium and small chain fatty ac-
ids? (Page 122)
A. Medium chain fatty acids do not require carnitine
for transport, so they are easily oxidised.
Q. What is the net generation of ATP, when one
molecule of palmitic acid (16 carbon) is oxidised
completely? (Page 123)
A. 129.
Q. What are the products, during each cycle of beta
oxidation of fatty acid? (Page 123)
A. Acetyl CoA, FADH2, and NADH.
Q. What are the energy producing steps in beta oxi-
dation pathway? (Page 123)
A. Fatty acyl CoA dehydrogenase (FAD) and beta
hydroxy fatty acyl CoA dehydrogenase (NAD)
steps.
Q. What is the product of beta oxidation of odd
chain fatty acids? (Page 124)
A. Propionyl CoA.
Lipids-II 97
Q. What is the further metabolism of propionyl

CoA? (Page 124)
A. Propionyl CoA is first carboxylated to methyl
malonyl CoA and then to form succinyl CoA. The
succinyl CoA then enters TCA cycle.
Q. What are the co-enzymes required for the con-
version of propionyl CoA to succinyl CoA?
(Page 124)
A. Biotin, ATP, Vitamin B12.
Q. Succinyl CoA is generated from which sub-
stances? (Page 124)
A. Odd chain fatty acids, propionic acid, valine, iso-
leucine, threonine.
Q. Succinyl CoA is utilised for what purposes?
(Page 124)
A. Porphyrin biosynthesis, activation of acetoacetate,
and oxidation in TCA cycle.
Q. What is alpha oxidation of fatty acid?(Page 124)
A. It is a process by which fatty acids are oxidised
by removing carbon atoms, one at a time, from
the carboxyl end. It is used for fatty acids that have
a methyl group at the beta-carbon, which blocks
beta-oxidation. Alpha oxidation does not gener-
ate energy.
Q. Where is alpha oxidation taking place?
(Page 124)
A. In endoplasmic reticulum (microsomes).
Q. Refsum’s disease is due to what? (Page 125)
A. Accumulation of phytanic acid, due to defective
alpha oxidation.
Q. What are the major differences between fatty acid

synthesis and beta oxidation of fatty acid?
(Page 125)
A. Beta oxidation is taking place in mitochondria,
fatty acid synthesis is in cytoplasm. Oxidation en-
zymes are independent, synthetic enzymes are
grouped as a multi-enzyme complex. During oxi-
dation, 2 carbon units are removed as acetyl CoA,
during synthesis, 2 carbon units are added as 3
carbon malonyl CoA. For oxidation, NAD and
FAD are necessary, for synthesis, NADPH is used.
Q. How NADPH is made available? (Page 128)
A. In the HMP shunt pathway, glucose-6-phosphate
dehydrogenase reaction produces NADPH.
Q. What is the rate limiting enzyme of de novo syn-
thesis of fatty acid? (Page 126)
A. Acetyl CoA carboxylase.
Q. What is the reaction? (Page 126)
A. Acetyl CoA + CO2 ® Malonyl CoA.
Q. What are the co-enzymes required for the reac-
tion? (Page 126)
A. Biotin and ATP.
Q. Acetyl CoA from mitochondria is transferred to
cytoplasm for the de novo synthesis of fatty acid,
by which enzyme? (Page 126)
A. ATP citrate lyase.
Q. What are the steps in which NADPH is used in
fatty acid synthesis? (Page 127)
A. Step 4 (Keto acyl reductase) and Step 6 (Enoyl re-
ductase).
Lipids-II 99
Q. Acetyl CoA is used for what purposes?

(Page 127)
A. Fatty acid synthesis, oxidation in citric acid cycle
for generation of energy, cholesterol synthesis and
ketone body formation.
Q. What are the sources of NADPH for fatty acid
synthesis? (Page 128)
A. Glucose-6-phosphate dehydrogenase, malic en-
zyme, cytoplasmic malate dehydrogenase.
Q. How is fatty acid synthesis regulated?
(Page 128)
A. Key enzyme, acetyl CoA carboxylase, is stimu-
lated by citrate and inhibited by palmitoyl CoA.
Q. What is the action of insulin on fatty acid syn-
thesis? (Page 128)
A. Insulin favours lipogenesis.
Q. How? (Page 128)
A. Insulin enhances the uptake of glucose by
adipocytes and increases the activity of pyruvate
dehydrogenase. So, availability of acetyl CoA is
increased. Insulin also activates glucose-6-phos-
phate dehydrogenase, so that enough NADPH is
available. Moreover, insulin stimulates acetyl
CoA carboxylase, the key enzyme of fatty acid
synthesis pathway. (Table 10.3). Insulin also de-
presses the hormone sensitive lipase (Fig.13.11).
Q. Chain elongation of fatty acid is taking place in
which site? (Page 128)
A. Microsomal elongation system is more active.
Q. Triacyl glycerol synthesis is enhanced by which

hormone? (Page 129)
A. Insulin.
Q. In adipose tissue, what is the source of glycerol
phosphate for triglyceride formation?(Page 129)
A. From dihydroxy acetone phosphate, derived from
glucose.
Q. White adipose tissue is concerned with what?
(Page 129)
A. Energy storage.
Q. Brown adipose tissue is involved in what pro-
cess? (Page 129)
A. Thermogenesis.
Q. What enzyme is involved in lipolysis?
(Page 129)
A. By hormone sensitive lipase.
Q. What is its action? (Page 129)
A. In adipose tissue, hormone sensitive lipase hy-
drolyses triglyceride into fatty acid and releases
into blood.
Q. In the blood, fatty acids are transported as what
form?
A. Albumin is the carrier of free fatty acid.
Q. Hormone sensitive lipase is activated by which
hormones? (Page 129)
A. Growth hormone, corticosteroids, ACTH,
adrenalin, and glucagon.
Lipids-II 101
Q. Which are the lipolytic hormones? (Page 129)

A. Growth hormone, corticosteroids, ACTH,
adrenalin, and glucagon.
Q. What is the mechanism of activation of hormone
sensitive lipase? (Page 129)
A. A cascade through adenyl cyclase, cyclic AMP and
kinase.
Q. What is the action of caffeine? (Page 129)
A. It inhibits phospho diesterase, increases activity
of hormone sensitive lipase, and so, prolongs the
action of cyclic AMP. Thus, caffeine favours li-
polysis.
Q. In diabetes mellitus, non-esterified fatty acid
level in blood is increased, why? (Page 129)
A. Insulin inhibits hormone sensitive lipase, in dia-
betes, this inhibition is removed, so, more lipoly-
sis is taking place.
Q. What worsens fatty liver? (Page 130)
A. Alcohol, diabetes mellitus, excess calorie intake,
hepatitis virus.
Q. What are the sources of acetyl CoA? (Page 130)
A. Pyruvate, fatty acids, acetoacetyl CoA, and leu-
cine.
Q. What substances will prevent fatty liver?
(Page 131)
A. Choline, methionine, lecithin.
Q. What are ketone bodies? (Page 131)
A. Aceto acetate, beta hydroxy butyric acid, and ac-
etone.
Q. Ketone bodies are formed in which tissue?

(Page 131)
A. Liver.
Q. Ketogenesis is taking place in which subcellular
organelle? (Page 131)
A. Mitochondria.
Q. What is the rate-limiting-step in ketone body
formation? (Page 131)
A. HMGCoA synthase.
Q. HMGCoA is directly converted into what sub-
stances? (Page 131)
A. Acetoacetate, acetyl CoA, mevalonate.
Q. Ketone body utilisation is taking place in which
organs? (Page 131)
A. Ketolysis is taking place in extra hepatic tissues.
(All other tissues, except liver).
Q. Utilisation of ketone bodies by peripheral tissues
needs which enzyme? (Page 131)
A. Succinyl CoA dependent thiophorase.
Q. Ketosis is due to what processes? (Page 132)
A. Step 1: Absence of insulin leads to excessive hy-
drolysis of triacyl glycerol. Step 2: So more fatty
acid is available, and more acetyl CoA is pro-
duced. Step 3: But oxidation of acetyl CoA in cit-
ric acid cycle is sluggish. The excess acetyl CoA
is diverted into ketone body formation.
Q. What test is used to identify ketone bodies in
urine? (Page 132)
A. Rothera’s test.
Lipids-III 103
Lipids-III:
Cholesterol, Lipoproteins
and Cardiovascular Diseases
Q. What is the ring structure present in cholesterol?

(Page 133)
A. Perhydro cyclo pentano phenanthrene ring.
Q. Cholesterol has how many carbon atoms?
(Page 133)
A. It has 27 carbon atoms.
Q. What are the substances derived from choles-
terol? (Page 133)
A. Glucocorticoids, mineralocorticoids, testosterone,
estrogen, bile acids.
Q. Which food stuffs contain cholesterol?
(Page 133)
A. Non-vegetarian food.
Q. Whether cholesterol is present in vegetable oils?
(Page 133)
A. No.
Q. What is the rate-limiting-step in the cholesterol

biosynthesis? (Page 134)
A. HMG CoA reductase.
Q. What is HMG CoA synthase? (Page 131)
A. It is the rate-limiting-enzyme in ketogenesis path-
way.
Q. What is the first sterol ring formed during cho-
lesterol biosynthesis? (Page 134)
A. Lanosterol.
Q. How cholesterol is excreted? (Page 135)
A. Through bile, partly as cholesterol itself, and
partly as bile salts.
Q. What is the normal level of total plasma lipids?
(Page 135)
A. 400-600 mg/dl.
Q. What is the normal level of total cholesterol?
(Page 135)
A. 150-220 mg/dl.
Q. What is the normal level of triglycerides?
(Page 135)
A. 50-200 mg/dl.
Q. How lipoproteins are estimated? (Page 136)
A. Either by electrophoresis or by ultracentrifuga-
tion.
Q. During electrophoresis, what is the fastest mov-
ing lipoprotein? (Page 136)
A. HDL (alpha lipoprotein).
Lipids-III 105
Q. During electrophoresis, what is the least mov-

ing lipoprotein? (Page 136)
A. Chylomicron (gamma position).
Q. Maximum cholesterol content is in which lipo-
protein? (Page 136)
A. LDL (Beta lipoprotein).
Q. Triglycerides present in chylomicrons are hy-
drolysed by what? (Page 137)
A. Lipoprotein lipase.
Q. Where is the enzyme present? (Page 137)
A. It is located at the endothelial layer of capillaries
of adipose tissue, muscles and heart, but not in
liver.
Q. What is the main apoprotein present in chylo-
micron. (Page 137)
A. B48.
Q. What is the function of chylomicron? (Page 137)
A. Transport of triglycerides from intestine to adi-
pose tissue.
Q. Highest content of triglycerides is seen in which
lipoprotein? (Page 137)
A. Chylomicrons.
Q. Endogenous triglycerides in plasma are carried
by what? (Page 138)
A. VLDL.
Q. What is the main apoprotein present in LDL?
(Page 138)
A. B100, it is the ligand for LDL receptor.
Q. What is the function of LDL receptors?

(Page 138)
A. LDL receptors are present on all cells but most
abundant in hepatic cells and adrenal cortex. LDL
receptors, located in specialised regions called
clathrin-coated pits. When the apo B-100 binds to
the receptor, the receptor-LDL complex is
internalised by endocytosis.
Q. What is the function of LDL? (Page 138)
A. Transport of cholesterol from liver to peripheral
tissues.
Q. What is “bad cholesterol”? (Page 139)
A. LDL cholesterol.
Q. Why it is called so? (Page 139)
A. LDL transports cholesterol from liver to periph-
eral tissues, where it is deposited, and causes ath-
erosclerosis.
Q. What is lipoprotein(a) ? (Page 139)
A. It is attached to apo B-100 by a disulfide bond. It
has significant homology with plasminogen. So
it interferes with plasminogen activation and im-
pairs fibrinolysis (Fig.14.10). This leads to unop-
posed intravascular thrombosis and possible myo-
cardial infarction.
Q. What is the significance of lipoprotein (a)?
(Page 139)
A. Lp(a) is associated with heart attacks at the age of
30 or 40 years. Indians have a higher level of Lp(a)
than Europeans.
Lipids-III 107
Q. What is the normal level of lipoprotein (a) ?

(Page 139)
A. In 40% population, there is no detectable level of
Lp(a) in serum. In 20% of population, the Lp(a)
concentration in blood is more than 30 mg/dl, and
these persons are susceptible to heart attack at a
younger age.
Q. What is the function of HDL? (Page 139)
A. Transport of cholesterol from peripheral tissues
to liver.
Q. What is “good cholesterol”? (Page 139)
A. HDL cholesterol.
Q. Why it is called so? (Page 139)
A. HDL transports cholesterol from peripheral tis-
sues to liver, and so helps in excretion of choles-
terol from the body. So HDL is anti-atherogenic.
Q. What is the main apoprotein present in HDL?
(Page 139)
A. Apo A-1, it is the ligand for HDL receptor.
Q. What is LCAT? (Page 139)
A. Lecithin cholesterol acyl transferase.
Q. Where is it present? (Page 139)
A. LCAT present in plasma is activated by apo-A1,
when LCAT binds to HDL disc.
Q. What is its importance? (Page 139)
A. The free cholesterol is esterified by LCAT the es-
terified cholesterol is then incorporated into HDL
disc, to form mature HDL. So for excretion of cho-
lesterol, LCAT is necessary.
Q. What is the importance of PUFA in cholesterol

metabolsim? (Page 140)
A. PUFA present in lecithin is transferred to choles-
terol by the enzyme LCAT. The esterified choles-
terol is then taken by HDL, and finally excreted
through liver. So, for excretion of cholesterol,
PUFA is required. Thus, PUFA will lower the
blood level of cholesterol.
Q. Free fatty acids of plasma are bound to what?
(Page 140)
A. Bound to serum albumin.
Q. What is the function of albumin? (Page 140)
A. Transport of free fatty acid from adipose tissue to
peripheral tissues.
Q. Triglycerides present in adipose tissue are hy-
drolysed by what enzyme? (Page 140)
A. Hormone sensitive lipase.
Q. What are the salient features of hyperlipoprotei-
nemia Type II-A? (Page 141)
A. Premature atherosclerosis elevated plasma LDL
cholesterol, and prominent beta band on electro-
phoresis.
Q. What is it due to? (Page 141)
A. Defect in LDL receptor.
Q. What is the treatment policy? (Page 141)
A. Low cholesterol diet, decreased intake of satu-
rated fat, increased intake of PUFA, bile acid bind-
ing resins.
Lipids-III 109
Q. What is the normal serum cholesterol level?

(Page 142)
A. 150-220 mg/dl.
Q. Hypercholesterolemia is seen in what conditions?
(Page 143)
A. Diabetes mellitus, nephrotic syndrome, obstruc-
tive jaundice, hypothyroidism.
Q. How atherosclerosis started? (Page 143)
A. The effect is directly proportional to the LDL lev-
els. Free radical induced oxidative damage of
LDL will accelerate this process. Oxidised LDL-
cholesterol is deposited in the subintimal regions
of arteries.
Q. What tissues are affected mostly by atheroscle-
rosis? (Page 143)
A. Aorta, coronary arteries and cerebral vessels are
predominantly affected.
Q. How LDL deposit leads to atherosclerosis?
(Page 143)
A. Oxidised LDL is taken up by macrophages, the
macrophages become overloaded with cholesterol
esters, and these are then called “foam cells” which
form the hallmark of atherosclerotic plaques.
Q. What happens to atherosclerotic plaque?
(Page 143)
A. This leads to narrowing of vessel wall. Then fibrous
proliferation takes place, this is due to liberation
of various growth factors. Again a clot is formed
which occludes one of the major vessels. Then there
is ischemia of the tissue supplied. Finally infarc-
tion or ischemic death of the tissue occurs.
Q. What are the important risk factors of coronary

artery diseases? (Page 144)
A. Serum cholesterol level above 220 mg/dl, LDL-
cholesterol level above 160 mg/dl, HDL-choles-
terol level below 35 mg/dl, and Apo(a) above 30
mg/dl.
Q. What are other risk factors associated with coro-
nary artery diseases? (Page 144)
A. Cigarette smoking, hypertension, diabetes melli-
tus, serum triglyceride level above 200 mg/dl,
homocysteine level, sedentary life style, obesity.
Q. What advise you will give to a person with in-
creased cholesterol level? (Page 144)
A. Reduce food with higher cholesterol content of
food, include PUFA and omega-3 fatty acids in
diet, reduction of total fat intake of green leafy
vegetables, exercise, avoid cigarettes.
Q. When will you start drugs for a person with in-
creased cholesterol level? (Page 144)
A. When patient’s condition is not responding to the
dietary restriction.
Q. What are the drugs available to treat hypercho-
lesterolemia? (Page 144)
A. Bile acid binding recins, HMGCoA reductase in-
hibitors, fibrate derivatives, nicotinic acid.
Q. What is the function of bile acids? (Page 146)
A. They are the major route of excretion of choles-
terol and they are required for absorption of
triacyl glycerol.
Lipids-III 111
Q. Bile acids are derived from what substance?

(Page 146)
A. Cholesterol.
Q. How are bile salts formed? (Page 146)
A. Bile acids conjugated with taurine or glycine.
Lipids-IV:
MCFA, PUFA and
Prostaglandins
Q. What is MCFA? (Page 147)

A. Medium chain fatty acids they contain 8 to 14 car-
bon atoms.
Q. What is LCFA? (Page 147)
A. Long chain fatty acids they contain 16 to 18 car-
bon atoms.
Q. What is VLCFA? (Page 147)
A. Very long chain fatty acids they contain 20 or more
carbon atoms.
Q. What is the difference in digestion of MCT from
that of LCFA?
A. MCT containing triglycerides are digested by
MCT-specific lipase. Pancreatic lipase and bile
salts are not required. (Page 147)
Lipids-IV 113
Q. What is the difference in absorption of MCFA

from that of LCFA?
A. MCFA is absorbed directly to blood (not to
lacteals, as in the case of LCFA). Further, after
absorption, MCFA is carried by albumin in blood,
whereas LCFA are absorbed as triglycerides and
carried by chilomicrons. (Page 147)
Q. So what is the advantage of MCFA? (Page 147)
A. MCFA are easily digested, easily absorbed, and
easily oxidised (when compared to LCFA).
Q. When palmitoleic acid (16 C, 1 double bond) is
completely oxidised, what is the net generation
of ATP molecules? (Page 147)
A. 127.
Q. When unsaturated fatty acids are oxidised, how
many ATP is formed?
A. The energy yield is less by 2 ATP molecules per
double bond, when compared to the correspond-
ing chain length saturated fatty acid. (Page 147)
Q. Why 2 ATP molecules are reduced? (Page 147)
A. Because, the FAD dependent dehydrogenation
(step 1 of beta oxidation) does not occur at the
double bond.
Q. Name polyunsaturated fatty acids. (Page 147)
A. Linoleic, linolenic and arachidonic acids.
Q. What are essential fatty acids? (Page 148)
A. Those cannot be synthesised by the body. So they
are to be provided in the diet.
Q. Name the essential fatty acids. (Page 148)

A. Linoleic and linolenic acids are the only fatty ac-
ids which cannot be synthesised in the body.
Q. Where does desaturation of fatty acid takes
place? (Page 148)
A. In the endoplasmic reticulum.
Q. What is the enzyme called? (Page 148)
A. Microsomal desaturase system.
Q. What are the important substances derived from
PUFA? (Page 148)
A. Prostaglandins, prostacycline, thromboxanes,
leukotienes, HPETE.
Q. What are the functions of PUFA? (Page 148)
A. Synthesis of prostaglandins, synthesis of phos-
pholipids and esterification of cholesterol.
Q. How prostaglandins are classified? (Page 149)
A. According to the attachment of different substitu-
ent groups to the ring, PGs are named with capi-
tal letters such as A, B, E and F. In the same series,
depending on number of double bonds on the
side chains they are denoted by a subscript after
the capital letter, e.g. PGE1, PGE2, PGE3, etc. Se-
ries 2 have two double bonds at 13-14 (trans) and
5-6 (cis). This is the most common variety.
Q. Prostaglandins are derived from what substance?
(Page 149)
A. Prostaglandins are derived from the PUFA. The
Series 2 (with two double bonds) are derived from
arachidonic acid. All naturally occurring PGs be-
long to the 2-series.
Lipids-IV 115
Q. Prostaglandins are stored in what form?

(Page 149)
A. As precursors, as membrane phospholipids.
Q. How prostaglandins are synthesised?(Page 149)
A. The arachidonic acid is released by the action of
phospholipase A2 on phospholipids prostaglan-
din synthesis is catalysed by prostaglandin H syn-
thase (PGHS). It contains two separate enzyme
activities, cyclo-oxygenase and peroxidase.
Q. How prostaglandin synthesis is regulated?
(Page 150)
A. The phospholipase is activated by epinephrine.
Steroids inhibit PL and prevent release of arachi-
donic acid from membranes.
Q. What is the importance of cyclo-oxygenase?
(Page 150)
A. Cyclo-oxygenase is activated by catecholamines
and inhibited by non-steroid anti-inflammatory
drugs (NSAIDS). Cyclo-oxygenase is a “suicide”
enzyme.
Q. What is the mechanism of action of aspirin?
(Page 150)
A. Aspirin acetylates serine in the active site and ir-
reversibly inhibits the cyclo-oxygenase.
Q. How is prostaglandins inactivated? (Page 150)
A. Prostaglandins have only very short half life, of
about 30 seconds. They are inactivated by the 15-
hydroxy-prostaglandin-dehydrogenase which
converts 15-OH group to keto group.
Q. What is the mechanism of action of prostaglan-

dins? (Page 150)
A. Prostaglandins are local hormones, and function
through G-protein coupled receptors In most tis-
sues, PGE increases cAMP level. But in adipose
tissue and in renal tubular cells, PGE lowers
cAMP level.
Q. What is the action of prostacyclin on vascular en-
dothelium? (Page 150)
A. Prostacyclin causes vasodilatation. It also inhib-
its platelet aggregation and has a protective ef-
fect on vessel wall against deposition of platelets.
Q. What is the effect of thromboxane? (Page 150)
A. Thromboxane (TXA2) is the main PG produced
by platelets. The major effects are vasoconstric-
tion and platelet aggregation. Prostacyclin and
thromboxane are opposing in activity.
Q. What is the precursor of leukotrienes?
(Page 151)
A. They are produced from arachidonic acid.
Q. What is its biological importance? (Page 151)
A. LT B4 is produced in neutrophils, it is the most
potent chemotactic agent. The slow reacting sub-
stance of anaphylaxis (SRS-A) contains LTC4,
LTD4 and LTE4. They cause smooth muscle con-
traction, constrict the bronchioles, increase capil-
lary permeability and produce vasoconstriction.
Lipids-IV 117
Q. What are VLCFAs? (Page 151)

A. Fatty acids having 20 or more carbon atoms are
called very long chain fatty acids (VLCFA). Eicosa
penta-enoic acid (EPA) (Timnodonic acid, C-20, 5
double bonds) and docosa hexa-enoic acid (DHA)
(cervonic acid, C-22, 6 double bonds) are good
examples of VLCFA.
Q. What is the importance of DHA? (Page 151)
A. DHA is synthesised linolenic acid. DHA can be
obtained from fish oils or from milk. DHA is es-
pecially required for the development of brain
and retina. Low levels of DHA in blood is seen in
patients with retinitis pigmentosa.
Lipids-V:
Compound Lipids
Q. How phospholipids are classified? (Page 152)

A. 1. Nitrogen containing glycero phosphatides, 2.
Non-nitrogen containing glycero phosphatides, 3.
Plasmalogens, 4. Phospho sphingosides 5.
Glycosphingolipids 6. Sulpholipids.
Q. What is Lecithin? (Page 152)
A. Phosphatidyl choline.
Q. What is phosphatidic acid? (Page 152)
A. Phosphatidic acid is made up of one glycerol to
which two fatty acid residues are esterified to car-
bon atoms 1 and 2 and the 3rd hydroxyl group is
esterified to a phosphoric acid.
Q. What is Cephalin? (Page 152)
A. Phosphatidyl ethanol amine.
Lipids-V 119
Q. What is Cardiolipin? (Page 152)

A. Diphosphatidyl glycerol.
Q. What is sphingomyelin? (Page 154)
A. All sphingolipids have the long aliphatic
aminoalcohol sphingosine which is attached to a
fatty acid in amide linkage to form a ceramide. A
common phosphosphingoside present abun-
dantly in the nervous system, is sphingomyelin.
It contains choline. Sphingomyelins are the only
sphingolipid that contain phosphate and have no
sugar moiety.
Q. What is a cerebroside? (Page 154)
A. Ceramide monohexoside.
Q. What is a globoside? (Page 154)
A. Ceramide oligosaccharides.
Q. What is lung surfactant? (Page 153)
A. It is produced by lung epithelial cells. Surfactant
decreases surface tension of the aqueous layer of
lung and prevents collapse of lung alveoli.
Q. What are the constituents of surfactants?
(Page 153)
A. Surfactants contain dipalmitoyl lecithin, phos-
phatidyl glycerol, cholesterol and surfactant pro-
teins A, B and C.
Q. What is its clinical significance? (Page 153)
A. Low levels of surfactant leads to respiratory dis-
tress syndrome (RDS), which is a common cause
of neonatal morbidity.
Q. Phospholipids can aggregate into what ?

(Page 153)
A. Micelle and liposome.
Q. What is the nitrogenous base present in lecithin?
(Page 153)
A. Choline.
Q. Cerebroside contains what? (Page 154)
A. Sphingosine, fatty acid, hexose.
Q. On hydrolysis of sphingomyelin, what are ob-
tained? (Page 154)
A. Sphingosine, fatty acid, phosphoric acid, choline.
Q. A ganglioside on hydrolysis, will give rise to
what? (Page 154)
A. Sphingosine, fatty acid, N-acetyl neuraminic acid.
Q. Name some lipid storage diseases. (Page 156)
A. Tay Sach’s disease, Niemann Pick’s disease,
Gaucher’s disease.
Q. Gaucher’s disease is due to the deficiency of
what? (Page 157)
A. Beta glucosidase.
Q. What is accumulated in Gaucher’s disease?
(Page 157)
A. Glucocerebroside.
Q. Niemann-Pick disease is due to the deficiency
of what? (Page 157)
A. Sphingomyelinase.
Lipids-V 121
Q. What is accumulated in Niemann-Pick disease?

(Page 157)
A. Sphingomyelin.
Q. Tay Sach’s disease is due to the deficiency of
what? (Page 157)
A. Hexosaminidase.
Q. What is accumulated in Tay Sach’s disease?
(Page 157)
A. Ganglioside.
Amino Acid
Metabolism-I:
General: Digestion,
Absorption, Transamination,
Urea
Q. What is the enzyme mainly responsible for pro-

tein digestion in stomach? (Page 158)
A. Pepsin.
Q. What is the action of pepsin? (Page 158)
A. It hydrolyses peptide bonds formed by carboxyl
groups of phenyl alanine, tyrosine, tryptophan
and methionine.
Q. How pepsinogen is activated? (Page 158)
A. Removal of N-terminal end by gastric hydrochlo-
ric acid.
Q. What are zymogens? (Page 158)
A. They are pro-enzymes, inactive at the time of se-
cretion, but will be activated in the gastro intesti-
nal tract.
Amino Acid Metabolism-I 123
Q. How the activation is effected generally?

(Page 158)
A. Activation is achieved by removing a small part
of the precursor molecules. Selective proteolysis
produces the catalytic site.
Q. What is its biological significance? (Page 158)
A. Zymogens prevent autodigestion of the cells.
Q. What is its clinical significance? (Page 158)
A. Acute pancreatitis results when trypsinogen is
activated prematurely.
Q. What are important enzymes in pancreatic juice?
(Page 158)
A. Pancreatic juice contains the endopeptidases
trypsin, chymotrypsin and elastase.
Q. How trypsinogen is activated? (Page 159)
A. The activation of trypsinogen is by removal of a
hexapeptide from N-terminal end by entero-ki-
nase (enteropeptidase) present on the intestinal
microvillus membranes.
Q. What is the action of trypsin? (Page 159)
A. It hydrolyses peptide bonds formed by carboxyl
groups of arginine and lysine.
Q. How chymotrypsinogen is activated? (Page 159)
A. It is activated by trypsin.
Q. What is an endopeptidase? (Page 159)
A. It acts on peptide bonds inside the protein mol-
ecule, so that the protein becomes successively
smaller and smaller units.
Q. Give some examples of an endopeptidase.

(Page 159)
A. Trypsin, pepsin.
Q. What are exopeptidases? (Page 159)
A. They act at one of the protein molecule, liberat-
ing amino acids sequentially, one at a time.
Q. Give an example exopepdases. (Page 159)
A. Carboxypeptidase.
Q. What is carboxypeptidase? (Page 159)
A. It is secreted by cells of intestinal villi, it is a
metallo-enzyme containing zinc, it is an endopep-
tidase, spliting off carboxy terminal bond of the
protein.
Q. What is required for absorption of amino acids?
(Page 160)
A. It needs the help of glutathione.
Q. What are cathepsins? (Page 160)
A. Intracellular proteases.
Q. What is ubiquitin? (Page 160)
A. It is necessary for intracellular protein breakdown.
Q. What are proteosomes? (Page 160)
A. Ubiquitin tagged proteins are degraded inside the
cells, with the help of proteosomes.
Q. In fasting state, nitrogen is transported from
muscle as what form?
A. In the fasting state, the muscle releases mainly
alanine and glutamine of which alanine is taken
up by liver and glutamine by kidneys.(Page 160)
Q. Transamination of glutamic acid produces what?

(Page 161)
A. Alpha keto glutaric acid.
Q. What is the co-enzyme necessary for transami-
nation reaction?
A. Pyridoxal phosphate. (Page 161)
Q. What are the physiological significance of tran-
samination? (Page 161)
A. It synthesises non-essential amino acids, it helps
in the equalisation of quantities of amino acids, it
is the first step of amino acid breaking down path-
ways.
Q. What is the clinical significance of transamina-
tion? (Page 161)
A. Transaminases are increased in blood in liver and
cardiac diseases.
Q. What is transdeamination? (Page 161)
A. Transamination takes place in all the cells of the
body, the amino group is transported to liver as
glutamic acid which is finally oxidatively deami-
nated in liver. Thus, the two components of the
reaction are physically far away, but physiologi-
cally they are coupled. Hence the term trans-
deamination.
Q. Transamination reaction of pyruvate with
glutamate results in the production of what sub-
stances? (Page 161)
A. Alanine and alpha keto glutarate.
Q. Which amino acid is oxidatively deaminated in

liver? (Page 162)
A. Glutamic acid.
Q. What is the reaction catalysed by glutamate de-
hydrogenase?
A. Glutamate alpha keto glutarate + ammonia.
(Page 162)
Q. What is the co-enzyme required for glutamate
dehydrogenase?
A. NAD. (Page 162)
Q. Nitrogen atoms in the urea is derived from what
precursors?
A. One from ammonia and another from aspartic acid.
(Page 163)
Q. Ammonia is immediately trapped in brain by
what? (Page 163)
A. Glutamine synthetase.
Q. What is the reaction catalysed by glutamine syn-
thetase? (Page 163)
A. Glutamic acid + ammonia ® glutamine, this re-
quires hydrolysis of ATP to ADP.
Q. What is the key enzyme of urea synthesis?
(Page 163)
A. Carbamoyl phosphate synthetase.
Q. What are the two carbamoyl phosphate syn-
thetases? (Page 164)
A. CPS-I is involved in urea synthesis, CPS-II is re-
quired for pyrimidine synthesis. CPS-I is seen in
mitochondria, while CPS-II is in cytosol.
Q. What is the normal blood urea level? (Page 165)

A. 20-40 mg/dl.
Q. Blood urea level is markedly increased in which
A. Renal diseases.
Q. What is the normal urinary excretion of urea?
(Page 165)
A. 15-30 mg/day.
Amino Acid
Metabolism-II:
Simple, Hydroxy and Sulfur
Containing Amino Acids
Glycine, Serine, Alanine,
Threonine, Methionine, Cysteine
Q. Glycine is used for synthesis of what com-

pounds? (Page 166)
A. Serine, Creatine, Purines, Heme, Glutathione, Bile
salts.
Q. For creatine synthesis, which amino acids are
used? (Page 167)
A. Glycine, arginine, methionine.
Q. Guanido acetic acid is formed in which tissue?
(Page 167)
A. Kidney.
Q. Guanido acetic acid is formed from what amino
acids? (Page 167)
A. Arginine + glycine.
Amino Acid Metabolism-II 129
Q. Where is creatine is synthesised? (Page 167)

A. In liver.
Q. What is the significance of creatinine?(Page 167)
A. Excretion is increased in muscle dystrophy.
Q. How creatinine is produced in the body?
(Page 167)
A. By spontaneous degradation of creatine phos-
phate.
Q. What are the sources of oxalic acid in urine?
(Page 168)
A. Ascorbic acid and glycine.
Q. What is the cause of hyper oxaluria? (Page 168)
A. Protein targeting defect.
Q. What are the important substances produced
from serine? (Page 168)
A. Glycine, pyruvate,cysteine,selenocysteine, cho-
line, phosphatidyl serine.
Q. On decarboxylation, serine will produce what?
(Page 169)
A. Ethanol amine.
Q. Choline is derived from what? (Page 169)
A. Serine.
Q. What is the product of transamination of ala-
nine? (Page 169)
A. Pyruvic acid.
Q. What is the significance of glucose-alanine cycle?

(Page 169)
A. During starvation, alanine is released from muscle,
and is taken up by liver. In liver alanine is tran-
saminated to pyruvate, and pyruvate undergoes
gluconeogenesis.
Q. What are important substrates for transmethyla-
tion reactions? (Page 170)
A. Guanido acetic acid, serine, nor-epinephrine, N-
acetyl serotonin.
Q. What is the methyl donor in transmethylation
reaction? (Page 170)
A. S-adenosyl methionine.
Q. Which amino acid has two optically active (asym-
metric) carbon atom? (Page 170)
A. Threonine.
Q. What are the functions of glutathione?
(Page 171)
A. Reduction of met-hemoglobin to hemoglobin,
keeping RBC membrane integrity, carrying amino
acids across membranes, and detoxification of
peroxidases.
Q. What is glutathione? (Page 171)
A. Gamma glutamyl cysteinyl glycine.
Q. Urine of a patient with homocystinuria will be
positive for which test?
A. Cyanide nitroprusside test. (Page 173)
Amino Acid Metabolism-II 131
Q. What is the defective enzyme in homocystinuria?

(Page 173)
A. Cystathionine synthase.
Q. What are the characteristic features of homo-
cystinuria? (Page 173)
A. Mental retardation, subluxation of lens, and
thrombosis.
Q. Homocystinuria is due to abnormal metabolism
of which amino acid? (Page 173)
A. Methionine.
Q. What is the defective enzyme in Cystathionuria?
(Page 173)
A. Cystathionase.
Amino Acid
Metabolism-III:
Acidic, Basic and Branched
Chain Amino Acids, Glutamic
acid, Glutamine, Aspartic acid,
Asparagine, Lysine, Nitric Oxide,
Valine, Leucine, Isoleucine
Q. What are the major functions of glutamic acid?
(Page 175)
A. Transamination, transdeamination, ammonia
trapping in brain, and production of gamma
amino butyric acid.
Q. Transamination reaction of pyruvate with
glutamate results in the production of what sub-
stances? (Page 175)
A. Alanine and alpha keto glutarate.
Q. Which amino acid is oxidatively deaminated in
liver? (Page 175)
A. Glutamic acid.
Q. What is the reaction catalysed by glutamate de-
hydrogenase?
A. Glutamate ® alpha keto glutarate + ammonia.
(Page 175)
Amino Acid Metabolism-III 133
Q. What is the co-enzyme required for glutamate

dehydrogenase?
A. NAD. (Page 175)
Q. Ammonia is immediately trapped in brain by
what? (Page 175)
A. Glutamine synthetase.
Q. What is the reaction catalysed by glutamine syn-
thetase? (Page 175)
A. Glutamic acid + ammonia ® glutamine, this re-
quires hydrolysis of ATP to ADP.
Q. What is the reaction catalysed by glutaminase?
(Page 176)
A. Glutamine ® glutamic acid + ammonia.
Q. Glutaminase enzyme is used for what purpose?
(Page 175)
A. Excretion of ammonia in kidney tubules.
Q. Transamination of glutamic acid will give rise to
what?
A. Alpha keto glutarate.
Q. Decarboxylation of glutamic acid will give rise
to what?
A. Gamma amino butyric acid.
Q. What is GABA?
A. It is an inhibitory neurotransmitter. Which is pro-
duced by decarboxylation of glutamic acid.
Q. Which will give rise to an inhibitory neurotrans-
mitter? (Page 175)
A. Glutamic acid.
Q. Glutamic acid can be formed from which amino

acids? (Page 175)
A. Histidine, arginine, proline, glutamine.
Q. Transamination of pyruvic acid will give rise to
what? (Page 175)
A. Alanine.
Q. Transamination of oxaloacetic acid will give rise
to what? (Page 175)
A. Aspartic acid.
Q. What are the functions of glutamine? (Page 176)
A. Ammonia trapping in brain (glutamic acid + am-
monia to glutamine), ammonia production in kid-
ney (glutamine to glutamic acid + ammonia), syn-
thesis of purine (Nitrogen 3 and 9), synthesis of
pyrimidine (3rd Nitrogen), synthesis of guanine
and cytosine (amino groups).
Q. Alpha amino group of aspartic acid is incorpo-
rated into which compounds? (Page 176)
A. Purines (1st nitrogen and 6th amino), pyrimidines
(1st nitrogen and C4,5,6), and urea.
Q. Which amino acids are required for both purine
and pyrimidine synthesis? (Page 176)
A. Aspartic acid, glutamine.
Q. What is asparaginase? (Page 176)
A. Enzyme catalysing the reaction asparaginase to
aspartic acid + ammonia.
Q. What is its function? (Page 176)
A. Ammonia production in kidney tubules.
Amino Acid Metabolism-III 135
Q. What is its clinical application? (Page 176)

A. It is an anticancer drug against leukemias and
lymphomas. The leukemia cells cannot synthesis
glutamine, and the available glutamine is de-
stroyed by glutaminase, leukemia cells will starve
and die.
Q. Lysine is deficient in which food stuffs?
(Page 176)
A. Lysine is deficient in cereals.
Q. Carnitine is synthesised from which amino acid?
(Page 177)
A. Lysine.
Q. Nitric oxide synthase system needs which co-
enzymes? (Page 178)
A. FAD, FMN, tetra hydro biopterine, NADPH.
Q. What are the iso-enzymes of nitric oxide syn-
thase? (Page 178)
A. Neuronal NOS, inducible NOS (macrophages) and
endothelial NOS.
Q. What are the major functions of nitric oxide?
(Page 178)
A. Vasodilatation, keeping the normal blood pres-
sure, inhibitioin of adhesion of platelets, memory
process in brain, bactericidal in macrophages.
Q. What is the precursor of nitric oxide? (Page 178)
A. Arginine.
Q. Which will give rise to polyamines? (Page 179)
A. Ornithine.
Q. What are polyamines? (Page 179)

A. Polyamines are putrescine, spermine and sper-
midine.
Q. What are the functions of polyamines?
(Page 179)
A. They are growth factors, their concentration is in-
creased in cancer.
Q. Name some mono amines. (Page 180)
A. Histamine, dopamine, and serotonin.
Q. What about glutamine? Is it an amine?
(Page 180)
A. No. Glutamine is an amide of glutamic acid.
Q. Valine enters in which metabolism? (Page 180)
A. Valine is glucogenic.
Q. Leucine enters in which metabolism?(Page 180)
A. Leucine is ketogenic.
Q. Isoleucine joins in which metabolism?
(Page 180)
A. Isoleucine is partly glucogenic and partly keto-
genic.
Q. Branched chain keto acids are excreted in urine
in what condition?
A. Maple syrup urine disease. (Page 180)
Q. What is the defect in maple syrup urine disease?
(Page 180)
A. Deficient decarboxylation of branched chain keto
acids.
Amino Acid Metabolism-IV 137
Amino Acid
Metabolism-IV:
Aromatic Amino Acids:
Phenyl alanine, Tyrosine,
Tryptophan, Histidine
Q. Which amino acids are both glucogenic and

ketogenic? (Page 181)
A. Phenyl alanine, tyrosine, tryptophan, and
isoleucine.
Q. What are the important substances synthesised
from tyrosine?
A. Melanin, thyroxine, epinephrine and nor-
epinephrine. (Page 182)
Q. What is the immediate precursor of norepine-
phrine? (Page 182)
A. Dopamine.
Q. In pheochromocytoma, urine contains what
substance? (Page 183)
A. Vanillyl mandelic acid.
Q. Phenyl alanine level in blood is increased in

what condition?
A. Phenyl ketonuria. (Page 183)
Q. What is the defective enzyme in phenyl ketonuria?
(Page 183)
A. Phenyl alanine hydroxylase.
Q. What are the co-enzymes required for phenyl
alanine hydroxylase?
A. NADH, NADPH, tetrahydro bioptrin. (Page 181)
Q. Phenyl alanine, on transamination will give rise
to what? (Page 183)
A. Phenyl pyruvate.
Q. What are the salient features of phenylketonuria?
(Page 184)
A. Mental retardation, hyperactivity, high blood
phenyl alanine.
Q. Phenyl pyruvic acid is excreted in urine in which
condition?
A. Phenyl ketonuria. (Page 184)
Q. Homogentisic acid is excreted in urine in which
condition?
A. Alkaptonuria. (Page 184)
Q. What is the defective enzyme in alkaptonuria?
(Page 184)
A. Homogentisic acid oxidase.
Q. Ochronosis is a manifestation of which condition?
(Page 184)
A. Alkaptonuria.
Q. What is associated manifestation of albinism?

(Page 184)
A. Nystagmus.
Q. A person’s urine was found to turn black on
standing and gave a positive Benedict’s test. He
is likely to have what condition? (Page 184)
A. Alkaptonuria.
Q. In phenyl ketonuria, urine will be positive for
what test? (Page 184)
A. Ferric chloride test.
Q. What is the defect in tyrosinemia type I (hepato-
renal tyrosinemia)?
A. Fumaryl acetoacetate hydrolase deficiency.
(Page 185)
Q. What is the defect in tyrosinemia type II (oculocu-
taneous tyrosinemia? (Page 185)
A. Deficiency of tyrosine amino transferase.
Q. Tryptophan is deficient in which food stuff?
(Page 185)
A. Maize and corn.
Q. Xanthurenic acid in urine is seen in which
A. Pyridoxal deficiency.
Q. What are the important substances produced
from tryptophan?
A. Serotonin, melatonin, niacin, alanine, and
acetoacetate. (Page 186)
Q. Which amino acid will give rise to a vitamin?

(Page 186)
A. Tryptophan.
Q. Serotonin is derived from which amino acid?
(Page 186)
A. Tryptophan.
Q. What are the characteristic features of malignant
carcinoid syndrome (argentaffinoma)?(Page 186)
A. Niacin deficiency, increased serotonin production,
increased hydroxy indole acetic acid excretion,
fluctuating hypertension.
Q. Pellagra is manifested in which conditions?
(Page 186)
A. Niacin deficiency, pyridoxal deficiency, trypto-
phan deficiency, and carcinoid syndrome.
Q. What is Hartnup’s disease? (Page 188)
A. Absorption of aromatic amino acids from intestine
as well as reabsorption from renal tubules are
defective. So tryptophan deficiency, and pellagra-
like symptoms are seen.
Q. Tryptophan is excreted in large quantities in
which condition?
A. Hartnup’s disease. (Page 188)
Q. In Hartnup’s disease, which test will give a
positive test? (Page 188)
A. Obermeyer test will be positive in urine.
Q. Indican in urine is tested by what method?

(Page 188)
A. Obermeyer test.
Q. What is indican? (Page 187)
A. Putrefaction product of tryptophan.
Q. What is the amino acid which has maximum
buffering capacity at physiological pH?
(Page 188)
A. Histidine.
Q. What is the decarboxylation product of histidine?
(Page 188)
A. Histamine.
Q. Which is the vasodialator produced from
histidine? (Page 188)
A. Histamine.
Q. What is the clinical significance of histamine?
(Page 188)
A. It is a powerful vasodilator and mediator of
anaphylaxis.
Q. What is Figlu excretion test? (Page 189)
A. In folic acid deficiency, there is a block in histidine
metabolism, and figlu is excreted in large
quantities in urine.
Q. What is figlu? (Page 189)
A. Formimino glutamic acid, it is a product of
histidine metabolism.
Amino Acid
Metabolism-V:
Inter-relations of
amino acid metabolisms,
One carbon metabolism,
Amino acidurias
Q. Tetra hydro folic acid is used for what purpose?

(Page 190)
A. It is the carrier of one carbon compounds.
Q. Name one carbon compounds? (Page 190)
A. Formyl, formimino, methenyl, hydroxymethyl,
methylene, and methyl.
Q. Which are the donors to one carbon pool?
(Page 191)
A. Serine, choline, glycine, tryptophan, histidine.
Q. One carbon units are used for synthesis of what?
(Page 191)
A. C2 of purine, C8 of purine, serine, dTMP, choline,
creatine, epinephrine.
Amino Acid Metabolism-V 143
Citric Acid Cycle 143
Q. Which is the purely ketogenic amino acid?

(Page 192)
A. Leucine.
Q. What are partially ketogenic and partially
glucogenic amino acids?
A. Phenyl alanine, tyrosine, tryptophan, isoleucine.
(Page 192)
Q. What are important aminoacidurias which cause
mental retardation? (Page 192)
A. Phenyl ketonuria, homocystinuria, maple syrup
urine disease.
Q. What is the defect in phenylketonuria?
(Page 192)
A. Deficiency of phenyl alanine hydroxylase.
Q. What is the defect in alkaptonuria? (Page 192)
A. Deficiency of homogentisic acid oxidase.
Q. What is the defect in homocystinuria (type 1)?
(Page 192)
A. Deficiency of cystathionine beta synthase.
Q. What is the defect in maple syrup urine disease?
(Page 193)
A. Deficiency of branched chain keto acid decar-
boxylase.
Q. What is the defect in cystathionuria? (Page 193)
A. Deficiency of cystathionase.
Citric Acid Cycle
Q. What are the steps in which carbon dioxide is

liberated, during the oxidation of glucose?
(Page 195)
A. Pyruvate dehydrogenase, isocitrate dehydro-
genase, alpha keto glutarate dehydrogenase.
Q. Acetyl CoA is produced from what substrates?
(Page 194)
A. Pyruvate, fatty acids, and leucine.
(Page 195)
A. Oxidation in TCA cycle, fatty acid synthesis,
cholesterol synthesis, and ketone body formation.
Q. Give examples of substrate level phosphoryla-
tion. (Page 195)
A. 1,3-bisphospho glycerate kinase, pyruvate kinase,
and succinate thiokinase.
Citric Acid Cycle 145
Q. Which is the substrate level phosphorylation step

in the TCA cycle?
A. Succinate thiokinase. (Page 194)
Q. What is the inhibitor of succinate dehydroge-
nase? (Page 197)
A. Malonate.
Q. Give examples of reactions in which NADH is
generated. (Page 197)
A. Pyruvate dehydrogenase, isocitrate dehydro-
genase, and alpha keto glutarate dehydrogenase.
Q. How many ATPs are generated per one rotation
of the citric acid cycle? (Page 197)
A. 12 ATP.
Q. What is the net yield of ATP from one molecule
of glucose in anaerobic glycolysis? (Page 79)
A. 2 ATP.
Q. What is the net yield of ATP from one molecule
of glucose in aerobic glycolysis? (Page 79)
A. 8 ATP.
Q. During complete oxidation, what is the net yield
of ATP from one glucose molecule? (Page 79)
A. 38 ATP.
Q. Which is the amphibolic pathway? (Page 197)
A. Citric acid cycle.
Q. How TCA cycle is regulated? (Page 198)
A. Availability of ATP, NAD+ and oxaloacetate.
Q. Succinyl CoA is formed from which substrates?

(Page 199)
A. Isoleucine, valine, methionine, andodd chain fatty
acids.
Q. Fumarate is produced from which substances?
(Page 199)
A. A. Arginino succinate B. Phenyl alanine.
Q. Alpha keto glutaric acid is formed from which
substances? (Page 199)
A. Glutamic acid, histidine, arginine, and proline.
Q. Aspartic acid enters the TCA cycle at which level?
(Page 199)
A. Oxalo acetate.
Q. In normal resting state, most of the glucose is
utilised by which tissue?
A. Brain. (Page 200)
Q. What is the approximate percentage of storage
form of energy (total fuel reserve) present in a
normal human body? (Page 200)
A. Fat 85%, glycogen 1%, protein 14%.
Q. During starvation, which substances are
increased in blood? (Page 201)
A. Ketone bodies, glucagon, and epinephrine.
Electron Transport Chain 147
Electron
Transport Chain
Q. Give examples of high energy compounds.

(Page 206)
A. ATP, GTP, creatine phosphate, 1,3-bis phospho
glycerate, phosphoenol pyruvate, acetyl CoA, and
succinyl CoA.
Q. On hydrolysis of 1 mole of ATP to ADP, the release
of energy will be approximately how much?
(Page 206)
A. 7 kCal.
Q. Where is respiratory chain located? (Page 207)
A. In the inner mitochondrial membrane.
Q. How is respiratory chain organised? (Page 207)
A. Components are organised into four complexes.
Q. What are the activities taking place inside
mitochondria? (Page 207)
A. Citric acid cycle, electron transport chain, and beta
oxidation fatty acid.
Q. Where are enzymes of citric acid cycle located?

(Page 207)
A. Fluid matrix contains enzymes of citric acid cycle.
Q. What is the function of Co-enzyme Q?
(Page 208)
A. It catalyses the electron transport from complex I
or II to complex III.
Q. Cytochrome oxidase is present in which complex?
(Page 209)
A. Complex IV.
Q. What are NAD+ linked dehydrogenases?
(Page 209)
A. Glyceraldehyde-3-phosphate dehydrogenase,
pyruvate dehydrogenase, alpha keto glutarate
dehydrogenase, isocitrate dehydrogenase, malate
dehydrogenase, beta hydroxy acyl CoA dehydro-
genase.
Q. What are FAD-linked dehydrogenases?
(Page 209)
A. Succinate dehydrogenase, and acyl CoA dehydro-
genase.
Q. Which cytochromes contain copper? (Page 209)
A. Cytochrome oxidase.
Q. What is valinomycin? (Page 210)
A. It acts as an ionophore, dissipates the proton
gradient, and so inhibits ATP synthesis.
Q. What is atractylocide? (Page 210)
A. It inhibits translocase, and inhibits ATP synthesis.
Electron Transport Chain 149
Q. What are the salient features of ATP synthase?

(Page 210)
A. It has two subunits, Fo is a proton channel, and
F1 has catalytic activity.
Q. How many ATP are produced in the oxidation
of one molecule of NADH? (Page 210)
A. Three.
Q. How many ATP are produced in the oxidation
of one molecule of FADH? (Page 210)
A. Two.
Q. Which is complex V of respiratory chain?
(Page 210)
A. ATP synthase.
Q. What is oligomycin? (Page 210)
A. It inhibits oxidative phosphorylation.
Q. Name some inhibitors of oxidative phosphory-
lation. (Page 211)
A. Oligomycin, carbon monoxide, and cyanide.
Q. Which inhibits electron transport chain at site 1?
(Page 211)
A. Barbiturate.
(Page 211)
A. Naphthoquinone.
(Page 211)
A. Carbon monoxide and cyanide.
Q. What is the cause for death due to cyanide

A. Cyanide inhibits cytochrome oxidase.
Q. Which is a physiological uncoupler? (Page 211)
A. Thyroxine.
Q. Which is the inborn error due to a mutation in
NADH-Q reductase?
A. Leber’s hereditary neuropathy (LHON).
(Page 211)
Plasma
Free Radical and Proteins
Anti-oxidants 151
Free Radicals
and Anti-oxidants
Q. Name the free radicals.

A. Superoxide anion radical, hydroperoxyl radical,
hydrogen peroxide, hydroxyl radical, lipid
peroxide radical, singlet oxygen, nitric oxide, and
peroxy nitrite.
Q. What are the important characteristics of reactive
oxygen species?
A. Extreme reactivity, short life span, generation of
new ROS by chain reaction, and damage to
various tissues.
Q. What are the enzymes generating ROS in
macrophages?
A. NADPH oxidase, superoxide dismutase, and
myeloperoxidase.
Q. What are the biological effects of ROS?

A. Protein damage, loss of function, lipid peroxi-
dation, membrane damage, mitochondrial
damage, DNA damage, cell death, mutation, and
cancer.
Q. What are the free radical scavinging enzymes?
A. Superoxide dismutase, glutathione peroxidase,
glutathione reductase, and catalase.
Q. ROS causes what diseases?
A. Chronic inflammation, rheumatoid arthritis, acute
inflammations, bronchopulmonary dysplasia,
respiratory distress syndrome, retrolental
fibroplasia, cataract, reperfusion injury, athero-
sclerosis, and peptic ulcer.
Q. Name important anti-oxidants.
A. Alpha tocopherol (Vitamin E), Vitamin C, Vitamin
A, and beta carotene.
Plasma Proteins 153
Plasma Proteins
Q. What is normal serum albumin level?(Page 216)

A. 3.5-5 mg/dl.
Q. What is the normal value of total proteins in
serum? (Page 216)
A. 6-8 g/100 ml.
Q. Edema due to hypoproteinemia is seen in which
conditions? (Page 217)
A. Cirrhosis liver, malnutrition, and nephrotic
syndrome.
Q. In blood, albumin carries what substances?
(Page 217)
A. Free fatty acids, bilirubin, salicylate, and calcium.
Q. What is the clinical application of albumin
carrying bilirubin? (Page 217)
A. Bilirubin and salicylate compete for binding to
albumin, and so it is not safe to give salicylate to
infants having hemolytic disease.
Q. What are the functions of albumin? (Page 217)

A. It maintains colloidal osmotic pressure of plasma,
and it transports non-esterified fatty acid and
bilirubin.
Q. Albumin is synthesised in which organ?
(Page 217)
A. Liver.
Q. Where is gamma globulins synthesised?
(Page 217)
A. By reticulo endothelial system (Spleen, lymph
nodes).
Q. Polymorphism is exhibited by which proteins?
(Page 218)
A. Haptoglobin, transferrin, and ceruloplasmin.
Q. Albumin globulin ratio is reversed in which
A. Cirrhosis, chronic infections, nephrotic syndrome,
and multiple myeloma.
Q. Name some transport proteins. (Page 218)
A. Transthyretin (thyroid hormones), retinol binding
protein, thyroxine binding globulin, transcortin
(cortisol), haptoglobin (hemoglobin), transferrin
(Iron), and hemopexin (free heme).
Q. Name acute phase proteins. (Page 219)
A. C-reactive protein, ceruloplasmin, and hapto-
globin.
Plasma Proteins 155
Q. What is the clinical manifestation of Alpha-1-

anti-trypsin deficiency? (Page 219)
A. Emphysema and chronic lung infections.
Q. What is ceruloplasmin? (Page 219)
A. It is a copper containing enzyme (ferroxidase)
seen in blood. It is an acute phase protein.
Q. What is the clinical significance of cerulo-
plasmin? (Page 219)
A. Ceruloplasmin level in blood is decreased in
Wilson’s hepatolenticular degeneration.
Q. What is the carrier protein of copper? (Page 219)
A. Albumin.
Q. Hemopexin carries what? (Page 220)
A. Free heme.
Q. How hemophilia is manifested? (Page 222)
A. Non-stopping hemorrhage after minor injuries.
Q. How hemophilia is transmitted? (Page 222)
A. It is inherited as an x-linked recessive trait, males
are affected, females are carriers.
Q. Hemorrhage tendency is seen in which condi-
tions? (Page 222)
A. Hemophilia, Vitamin K deficiency, and thrombo-
cytopenia
Immunochemistry
Q. How immunoglobulins are classified?

(Page 225)
A. IgG, IgM, IgA, IgD and IgE.
Q. What is the basic structure of an immunoglo-
bulin? (Page 225)
A. Two heavy chains and two light chains connected
by disulphide linkages.
Q. The antigen binding capacity of immunoglobulin
resides at which region of immunoglobulin?
(Page 225)
A. Variable region.
Q. What is primary response antibody? (Page 226)
A. Immunoglobulin M.
Q. What is the secondary response antibody?
(Page 226)
A. Immunoglobulin G.
Heme Synthesis
Immunochemistry
and Breakdown 157
Q. Which antibody is seen in body secretions?

(Page 227)
A. Immunoglobulin A.
Q. What is the clinical importance of immunoglo-
bulin E? (Page 227)
A. They mediate anaphylactic reaction.
Q. What is the cause of anaphylactic reaction?
(Page 227)
A. IgE attach on mast cells, when antigen is
introduced, antigen antibody reaction occurs, and
leading to mast cell degranulation.
Q. What is M band? (Page 228)
A. A narrow peak in gamma globulin, caused by
monoclonal antibodies secreted by malignant
plasma cells.
Q. What is Bence Jones protein? (Page 228)
A. It is the light chains of immunoglobulins, excreted
in urine. It is seen in urine of 20% cases of multiple
myeloma.
Q. What is the test done to detect Bence Jones
protein? (Page 228)
A. It is precipitated when heated between 45 and 60
degrees.
Q. How antibody diversity is produced?(Page 230)
A. By somatic recombination.
Specialised Proteins:
Collagen, Myosin
Q. What is the structural arrangement of collagen?

(Page 233)
A. It has triple stranded quarter staggered
arrangement. One-third residues are glycine.
About 1% residues are proline and hydroxy
proline.
Q. What are the post-translational modifications
taking place in collagen?
A. Hydroxylation of proline and lysine residues, and
hydrolysis of pro-collagen. (Page 233)
Q. Hydroxylation of proline and lysine needs what?
(Page 233)
A. It depends on vitamin C.
Q. In ascorbic acid deficiency, what happens?
(Page 233)
A. Poor hydroxylation, defective collagen and
scurvy.
Specialised
HemeProteins:
SynthesisCollagen
and Breakdown
Myosin 159
Q. Cross links in collagen are formed by what?

(Page 234)
A. It is formed between lysine and hydroxy lysine
residues. It is called desmosine.
Q. What is the enzyme for cross linkage formation?
(Page 234)
A. Lysyl oxidase.
Q. What is its clinical application? (Page 234)
A. Lysyl oxidase contains copper. So, in copper
deficiency lysine cross-link formation is deficient,
leading to defective collagen.
Q. What are inherited disorders leading to defective
collagen formation?
A. Osteogenesis imperfecta, Ehlers-Danlos synd-
rome, dermatoparaxis, homocystinuria, and
marfan’s syndrome. (Page 234)
Q. What is myosin? (Page 236)
A. It is a specialised protein seen in muscle.
Q. What is its biological function? (Page 236)
A. It can bind actin to form actomyosin. It has ATPase
activity.
Q. What is the function of Troponin-C ? (Page 237)
A. It binds calcium.
Q. What is the function of Troponin-I ? (Page 237)
A. ATPase inhibitory element.
Q. What is the clinical significance of Troponin-T ?
(Page 237)
A. Its serum level is increased in myocardial
infarction.
Heme Synthesis
and Breakdown
Q. What is the chemical structure of heme?

(Page 240)
A. It is ferro protoporphyrin.
Q. What are the substituent groups of heme?
(Page 240)
A. Methyl, vinyl, and propionyl groups.
Q. Heme is synthesised from what substances?
(Page 241)
A. It is synthesised from glycine and succinyl CoA.
Q. What is the rate limiting enzyme of heme
A. ALA synthase.
Q. Which enzyme is inhibited by lead? (Page 241)
A. ALA dehydratase and ferrochelatase.
Q. Methenyl bridge of protoporphyrin is derived
from what? (Page 241)
A. Alpha carbon of glycine.
Heme Synthesis and Breakdown 161
Q. How is heme synthesis regulated? (Page 242)

A. ALA synthase is repressed by heme, and ALA
synthase is allosterically inhibited by hematin.
Q. What is the action of barbiturates on heme
A. Barbiturates will induce heme synthesis.
Q. What is the treatment for acute intermittent
porphyria? (Page 243)
A. High carbohydrate diet, and stoppage of barbitu-
rates.
Q. What is the defect in acute intermittent porphyria?
(Page 243)
A. PBG-deaminase.
Q. How porphyrins are detected? (Page 243)
A. They show fluorescence under ultra violet light.
Q. In acute intermittent porphyria, urine contains
what? (Page 243)
A. ALA and PBG.
Q. Lead poisoning results in elevated levels of
what? (Page 244)
A. Delta amino levulinic acid.
Q. Degradation of heme needs which enzyme?
(Page 245)
A. Heme oxygenase system, with NADPH.
Q. Degradation of heme to bilirubin releases what
gas? (Page 245)
A. Carbon monoxide.
Q. Heme is converted to bilirubin in which site?

(Page 245)
A. Microsomes of reticulo-endothelial cells.
Q. Bilirubin in blood is carried by what?(Page 245)
A. Albumin.
Q. How it is made water soluble? (Page 245)
A. By conjugation with glucuronic acid.
Q. Where is the conjugation taking place?
(Page 245)
A. In liver.
Q. What is the enzyme? (Page 245)
A. UDP-glucuronyl transferase.
Q. What is the normal level of plasma bilirubin?
(Page 246)
A. 0.2-0.8 mg/dl.
Q. What is the normal level of conjugated bilirubin
in plasma? (Page 246)
A. Less than 0.2 mg /dl.
Q. What is latent jaundice? (Page 246)
A. When plasma bilirubin is between 1 to 2 mg/dl.
Q. What is jaundice? (Page 246)
A. When plasma bilirubin is more than 2 mg/dl, it
diffuses into tissues, causing yellowish discolou-
ration of tissues.
Q. Enterohepatic circulation is seen in which
A. Urobilinogen and bile salts.
Heme Synthesis and Breakdown 163
Q. What is the defect in Gilbert’s disease?

(Page 247)
A. Uptake of bilirubin by the liver is defective.
Q. What is the defect in Criggler-Najjar syndrome?
(Page 247)
A. Defect in conjugation of bilirubin due to
deficiency of UDP glucuronyl transferase.
Q. Conjugated hyperbilirubinemia is seen in which
A. Dubin Johnson’s syndrome.
Q. Bilirubin in serum is estimated by what test?
(Page 247)
A. Van den Bergh reaction.
Q. What is Direct van den Bergh’s reaction?
(Page 247)
A. The colour is developed immediately when blood
is added.
Q. What is your inference, when direct test is
positive? (Page 247)
A. Blood contains conjugated bilirubin, it is water
soluble.
Q. What is indirect van den Bergh’s test?(Page 247)
A. When blood is added to the solution, there is no
colour, but when alcohol is added, colour is
developed.
Q. What is the reason for this type of reaction?
(Page 247)
A. Bilirubin is soluble in alcohol, and alcohol extract
gives the reaction.
Q. What is kernicterus? (Page 248)

A. In young children, when plasma bilirubin is more
than 20 mg/dl, it diffuses into brain, causing
permanent damage to brain cells.
Q. In obstructive jaundice, what is seen in blood?
(Page 248)
A. Conjugated bilirubin in excess quantity.
Q. Bile salts and bile pigments are excreted in urine
in which condition?
A. Obstructive jaundice. (Page 248)
Q. Increased urobilinogen in urine is seen in which
A. Congenital spherocytosis, mismatched transfu-
sion, Rh incompatibility, auto-immune hemolysis,
and glucose-6-phosphate dehydrogenase
deficiency.
Haemoglobins 165
Haemoglobins
Q. What are the salient structural features of

hemoglobin molecule?
A. Hb has four subunits, two alpha and two beta
units. It contains four iron atoms.
Q. How many molecules of oxygen can bind with
hemoglobin?
A. Hb can bind four molecules of oxygen.(Page 249)
Q. 100 ml of blood can carry how much oxygen?
(Page 250)
A. 20 ml.
Q. What is Bohr effect? (Page 251)
A. The influence of pH and pCO2 to facilitate
oxygenation of Hb in the lungs and deoxyge-
nation at the tissues is known as the Bohr effect.
Q. What is chloride shift? (Page 251)
A. When CO2 is taken up, chloride ions from the
plasma would enter. This is called chloride shift
or Hamburger effect.
Q. Hemoglobin carries how much CO2? (Page 251)

A. Seventy five percent as isohydric transport and
15% as carbamino hemoglobin.
Q. What are the forms in which carbon dioxide is
transported? (Page 251)
A. Dissolved form, isohydric transport, and
carbamino hemoglobin.
Q. What is isohydric transport of carbon dioxide?
(Page 251)
A. There is minimum change in pH during the
transport.
Q. How this is effected? (Page 251)
A. The H+ ions are buffered by the deoxy-Hb.
Q. Which will decrease the affinity of hemoglobin
for oxygen?
A. 2,3-BPG level. (Page 252)
Q. What is the structural difference between HbA
and HbF?
A. HbA has two alpha and two beta chains, but HbF
has two alpha and two gamma chains.(Page 252)
Q. What are the laboratory tests to identify HbF?
(Page 252)
A. HbF moves slower than HbA on electrophoresis,
HbF is alkali resistant.
Q. What is the physiological significance of HbF?
(Page 252)
A. Oxygen affinity is more for HbF than HbA. HbF
is seen in foetal circulation.
Haemoglobins 167
Q. What is the clinical significance of HbF?

(Page 252)
A. It is seen in adults in hemoglobinopathies and
thalassemias.
Q. Why carbon monoxide becomes a poison?
(Page 253)
A. Hb has more affinity to carbon monoxide than
oxygen.
Q. What is the treatment for carbon monoxide
poison? (Page 253)
A. Hyperbaric oxygen.
Q. Met-hemoglobin is found in which conditions?
(Page 253)
A. Ingestion of nitrites, presence of HbM, GPD
deficiency.
Q. What is met-hemoglobin? (Page 253)
A. Hemoglobin in which iron is in ferric state.
Q. What is the defect of met-hemoglobin?
(Page 253)
A. It cannot release oxygen in tissues.
Q. What is the reagent used for colourimetric
estimation of hemoglobin? (Page 254)
A. Drabkin’s reagent, to convert Hb to cyanmet-
hemoglobin.
Q. What is hemoglobin S? (Page 254)
A. The glutamic acid in the 6th position of beta chain
of HbA is changed to valine in HbS.
Q. What is the cause for sickle cell anemia?

A. Solubility of deoxy HbS is lower than deoxy HbA,
so HbS is precipitated intracellularly, leading to
sickle shape of RBC.
Q. How HbS is identified?
A. HbS is slower moving on electrophoresis than
HbA.
Q. What is sickle cell trait?
A. Heterozygous (AS) condition, one allele is
normal, the other is abnormal, so half of Hb
molecules are normal, and half abnormal.
A. Sickle cell trait persons will not have any disease
manifestations, usually. But, at higher altitudes,
hypoxia may cause manifestation of the disease.
Chronic lung disorders may also produce
hypoxia-induced sickling in HbS trait.
Vitamin-I 169
Vitamin-I:
Fat Soluble
Vitamins: A, D, E and K
Q. What is the pro-Vitamin for Vitamin A?

(Page 259)
A. Beta carotene present in plants.
Q. What is the major function of Vitamin A?
(Page 260)
A. In vision, as the Wald’s visual cycle.
Q. What causes the nerve impulse in retina?
(Page 260)
A. Photo-isomerisation of 11-cis retinal to all trans-
retinal.
Q. How is all trans-retinal regenerated? (Page 261)
A. Trans-retinal is taken to liver, where it is made to
trans-retinol, then isomerised to cis-retinol and
then to cis retinal.
Q. What are the enzymes required for this regenera-
tion? (Page 261)
A. Alcohol dehydrogenase and retinol isomerase.
Q. What are other minor biological roles of Vitamin

A? (Page 262)
A. Normal maintenance of epithelium and skin,
glycoprotein synthesis, reproduction, cell
differentiation, and anti-oxidant role.
Q. What are the sources of Vitamin A? (Page 262)
A. Carrot, mangoes, papaya, green leafy vegetables,
and fish liver oil.
Q. What are the deficiency manifestations of
Vitamin A? (Page 262)
A. Night blindness, xerophthalmia, keratomalacia,
and keratinisation of epithelium.
Q. Nyctalopia is due to the deficiency of which
Vitamin? (Page 262)
A. Vitamin A.
Q. What is the daily requirement of Vitamin A?
(Page 263)
A. 750 to 1000 microgram.
Q. How cholecalciferol is synthesised? (Page 263)
A. From 7-dehydro cholesterol in the malpighian layer
of epidermis, by the action of ultra violet rays.
Q. How Vitamin D is activated? (Page 264)
A. Cholecalciferol from skin reaches liver. There it
is hydroxylated to form 25-hydroxy cholecalciferol
(25-HCC). It then reaches kidney, where further
hydroxylation takes place to form 1,25-dihydroxy
cholecalciferol (DHCC).
Vitamin-I 171
Q. What is calcitriol? (Page 264)

A. 1,25-dihydroxy cholecalciferol, or active Vitamin
D, contains three hydroxyl groups at 1, 3 and 25
positions. So it is called calcitriol.
Q. Which Vitamin acts as a pro-hormone?
(Page 264)
A. Vitamin D.
Q. What is the function of Vitamin D? (Page 264)
A. It increases absorption of calcium from intestine,
and it also increases mineralisation of bone.
Q. How Vitamin D increases absorption of calcium?
(Page 264)
A. Calcitriol binds to a cytoplasmic receptor. The
hormone-receptor complex interacts with DNA
and causes transcription of specific genes that
code for calbindin. Due to the increased
availability of calcium binding protein, the
absorption of calcium is increased.
Q. How is Vitamin D deficiency manifested?
(Page 265)
A. Rickets in children and osteomalacia in adults.
Q. In renal disease, oral doses of Vitamin D may
not be effective, why? (Page 265)
A. Hydroxylation and activation of Vitamin is taking
place in kidney.
Q. What are the causes of rickets? (Page 265)
A. Chronic renal failure, liver diseases, and under-
exposure to sunlight.
Q. What is the daily requirement of Vitamin D?

(Page 265)
A. 5-10 microgram.
Q. What is the chemical nature of Vitamin E?
(Page 265)
A. Alpha tocopherol.
Q. What is the function of Vitamin E ? (Page 266)
A. Anti-oxidant.
Q. What is the relationship of selenium with Vita-
min E? (Page 266)
A. They act synergistically as anti-oxidants.
Q. What is the source of Vitamin E? (Page 266)
A. Vegetable oils are rich sources of Vitamin E, e.g.
wheat germ oil, sunflower oil, safflower oil, cotton
seed oil, and palm oil.
Q. What is the normal daily requirement of Vitamin
E? (Page 266)
A. 15 mg or 33 international units.
Q. What is the chemical nature of Vitamin K?
(Page 266)
A. Naphthoquinone derivative.
Q. What is menadione? (Page 266)
A. It is synthetic water soluble Vitamin K, widely
used in clinical practice.
Q. What is the function of Vitamin K? (Page 267)
A. Gamma carboxylation of clotting factors such as
prothrombin.
Vitamin-I 173
Q. Deficiency of Vitamin K can occur in which

A. Obstructive jaundice, antibiotic therapy, and
administration of dicoumarol.
Q. What is the mechanism of action of dicoumarol?
(Page 267)
A. It competitively inhibits Vitamin K epoxide
reductase.
Q. So, dicoumarol is used for what purpose?
(Page 267)
A. To prevent intravascular thrombosis.
Q. Excess dicoumarol will produce what?(Page 267)
A. Bleeding tendency.
Q. Which substance will inhibit Vitamin K?
(Page 267)
A. Dicoumarol.
Q. Excess dose of Vitamin K in neonates may lead
to which condition?
A. Hemolysis and jaundice. (Page 267)
Q. Bleeding tendency is common in the deficiency
of which? (Page 267)
A. Vitamin K, Vitamin C, and platelets.
Vitamin-II:
Water soluble vitamins
Q. What is the source of thiamine? (Page 268)

A. Aleurone layer of cereals (food grains) is a rich
source of thiamine. Whole wheat flour and
unpolished rice and yeast are very good sources.
Q. Thiamine pyrophosphate is required for which
reactions ? (Page 268)
A. Transketolase, pyruvate dehydrogenase, and
alpha keto glutarate dehydrogenase.
Q. Which Vitamin is required for oxidative
decarboxylation? (Page 268)
A. Thiamine pyrophosphate.
Q. In thiamine deficiency, what alterations are seen
in blood ? (Page 269)
A. Increased pyruvic acid level and increased
transketolase activity.
Vitamin-II 175
Q. What are the clinical manifestations of thiamine

deficiency? (Page 269)
A. Beriberi, Wernick’s syndrome, and polyneuritis.
Q. Beberi is due to the deficiency of which Vitamin?
(Page 269)
A. Thiamine.
Q. What is the daily requirement of Vitamin B1
(thiamine) ? (Page 269)
A. 1 to 1.5 milligram.
Q. Chronic alcoholism may lead to the deficiency
of which Vitamin?
A. Vitamin B1. (Page 269)
Q. Wernicke’s encephalopathy is due to the
deficiency of which Vitamin?
Q. What is the co-enzyme function of riboflavin ?
(Page 269)
A. FMN and FAD dependent enzymes.
Q. What are the FAD dependent enzymes?
(Page 270)
A. Succinate dehydrogenase, acyl CoA dehydro-
genase, xanthine oxidase, glutathione reductase,
glycine cleavage system, pyruvate dehydro-
genase, and alpha ketoglutarate dehydrogenase.
Q. What are the manifestations of riboflavin
A. Glossitis, cheilosis, angular stomatits, and
circumcorneal vascularisation.
Q. What is the dietary sources of riboflavin?

(Page 270)
A. Rich sources are liver, dried yeast, egg, and milk.
Q. What is the daily requirement of riboflavin?
(Page 270)
A. 1.5 mg per day.
Q. Which Vitamin is synthesised in the body?
(Page 271)
A. Niacin.
Q. What is the co-enzyme function of niacin?
(Page 271)
A. NAD and NADP.
Q. Name some important NAD dependent enzymes.
(Page 271)
A. Lactate dehydrogenase, glyceraldehyde-3-
phosphate dehydrogenase, pyruvate dehydro-
genase, beta hydroxy acyl CoA dehydrogenase,
and mitochondrial isocitrate dehydrogenase.
Q. Name the NADPH generating reactions.
(Page 271)
A. Glucose-6-phosphate dehydrogenase, 6-phospho
gluconate dehydrogenase, malic enzyme, and
cytoplasmic isocitrate dehydrogenase.
Q. What are the important NADPH utilising
reactions? (Page 271)
A. Beta keto acyl ACP dehydrogenase, alpha, beta
unsaturated ACP dehydrogenase, HMGCoA
reductase, met-hemoglobin reductase, dihydrofo-
late reductase, and phenylalanine hydroxylase.
Vitamin-II 177
Q. Pellagra is seen in the deficiency of which

Vitamin? (Page 271)
A. Niacin.
Q. What are the features of pellagra ? (Page 271)
A. Dermatitis, diarrhea, and dementia.
Q. What is the precursor of niacin? (Page 271)
A. Tryptophan.
Q. Tryptophan will give rise to how much niacin?
(Page 272)
A. About 60 mg of tryptophan will yield 1 mg of niacin.
Q. Tryptophan is deficient in which food stuff?
(Page 272)
A. Maize and corn.
Q. Which conditions will lead to symptoms of
pellagra? (Page 272)
A. Isoniazid therapy, low tryptophan content in diet,
niacin deficiency, hartnup disease, and carcinoid
syndrome.
Q. What is the dietary sources of niacin?(Page 272)
A. Natural sources of niacin are dried yeast, rice poli-
shing, liver, peanut, whole cereals, legumes, meat
and fish. About half of the requirement is met by
the conversion of tryptophan to niacin. About 60
mg of tryptophan will yield 1 mg of niacin.
Q. What is the daily requirement of niacin?
(Page 272)
A. The R.D.A is 20 mg/day.
Q. Transamination reaction requires which

Vitamin? (Page 272)
A. Pyridoxal phosphate.
Q. Pyridoxal phosphate is required for what
reactions? (Page 272)
A. Transamination reactions, decarboxylation of amino
acids, ALA synthase, glycogen phosphorylase.
Q. Give an example of transamination reaction.
(Page 272)
A. Alanine transaminase (ALT) will catalyse the
reaction, alanine to pyruvate.
A. Blood level of ALT is increased in liver diseases,
AST is increased in myocardial infarction.
Q. Give some examples of decarboxylation reactions.
(Page 273)
A. Glutamate to GABA (gamma aminobutyric acid),
histidine to histamine, 5-hydroxy tryptophan to
serotonin, cysteine to taurine, and serine to
ethanol amine.
Q. Xanthurenic acid in urine is seen in the deficiency
of which Vitamin?
A. Pyridoxal deficiency. (Page 273)
Q. What are the manifestations of pyridoxal
A. Infantile convulsions, peripheral neuritis,
pellagra, and anemia.
Vitamin-II 179
Q. What is the reason for infantile convulsions in

pyridoxal deficiency?
A. Pyridoxal phosphate is required for the forma-
tion of GABA, and it is an inhibitory neurotrans-
mitter, absence of which leads to hyper-excitation
and convulsions. (Page 273)
Q. What is the reason for peripheral neuritis in
A. PLP is involved in the synthesis of sphingolipids,
so B6 deficiency leads to demyelination of nerves
and consequent peripheral neuritis. (Page 273)
Q. What is the reason for pellagra-like disease in
A. Since niacin is produced from tryptophan, one of
the enzymes of this pathway is PLP dependent.
So B6 deficiency in turn leads to niacin deficiency
which is manifested as pellagra. (Page 273)
Q. Can you give an exmple of one Vitamin defi-
ciency leading to another Vitamin deficiency?
(Page 273)
A. PLP deficiency in turn leads to niacin deficiency
which is manifested as pellagra.
Q. What is the reason for anemia in pyridoxal
A. PLP is required for ALA synthase. In adults
hypochromic microcytic anemia may occur due
to the inhibition of heme biosynthesis.
Q. What are the drugs which cause pyridoxal

A. Isonicotinic acid hydrazide (INH) (isoniazid),
cycloserine, penicillamine and oral contracep-
tives act as B6 antagonists. Ethanol in the body is
converted to acetaldehyde, which inactivates PLP.
Q. What are the dietary sources of pyridoxal?
(Page 274)
A. Rich sources are yeast, rice polishing, wheat
germs, cereals, legumes (pulses), egg, milk, meat,
fish and green leafy vegetables.
Q. What is the daily requirement of pyridoxal
phosphate? (Page 274)
A. 1 to 2 mg/day.
Q. What is the co-enzyme form of pantothenic acid?
(Page 274)
A. Co-enzyme A.
Q. What is the function of CoA? (Page 274)
A. Oxidation of pyruvic acid and activation of acyl
groups.
Q. Deficiency of pantothenic acid leads to what?
(Page 274)
A. Burning foot syndrome.
Q. What are the donors for acetyl CoA pool?
(Page 275)
A. Pyruvate, fatty acid, and amino acids.
Vitamin-II 181

(Page 275)
A. Oxidation in TCA cycle, fatty acid synthesis,
cholesterol synthesis, steroid synthesis, and
ketone body formation.
Q. Succinyl CoA is used for what purposes?
(Page 275)
A. Oxidation in TCA cycle, heme synthesis, and
activation of acetoacetate.
Q. What is the function of biotin? (Page 275)
A. Carboxylation reactions.
Q. Name some reactions dependent on biotin.
(Page 275)
A. Acetyl CoA carboxylase, propionyl CoA
carboxylase, and pyruvate carboxylase.
Q. What is the antagonist for biotin? (Page 276)
A. Avidin.
Q. What is its use in laboratory? (Page 276)
A. Biotin-avidin reaction is used in immunosorbent
assays.
Q. What is the chemical nature of folic acid?
(Page 276)
A. Pteroyl glutamic acid (pteridine + PABA + gluta-
mic acid).
Q. What is PABA? (Page 276)
A. Para amino benzoic acid.
Q. What is the co-enzyme form of folic acid?

(Page 276)
A. Tetrahydro folic acid.
Q. What is the main function of folic acid?
(Page 276)
A. Tetrahydro folic acid is the carrier of one carbon
units.
Q. What are the causes of folate deficiency?
(Page 277)
A. Pregnancy, defective absorption (sprue, celiac
disease), anticonvulsant drugs (hydantoin,
dilantin, phenytoin, phenobarbitone), hemolytic
anemias, and dietary deficiency.
Q. What is the major manifestation of folic acid
deficiency?
A. Macrocytic anemia. (Page 277)
Q. Folic acid deficiency in pregnancy is associated
with what? (Page 277)
A. Folic acid deficiency during pregnancy may lead
to neural tube defects in the fetus. Folic acid
prevents birth defects (fetal malformations such
as spina bifida).
Q. What are the other minor effects of folic acid?
(Page 277)
A. Folic acid is also useful to reduce the level of
homo-cysteine in blood, and therefore helps in
preventing heart diseases. Folic acid is beneficial
in prevention of cancer.
Vitamin-II 183
Q. What are the laboratory findings in folic acid

A. (1) Normal folic acid level in serum is decreased.
(2) FIGLU is excretion is more, especially after
histidine load. (3) AICAR excretion in urine. (4) Peri-
pheral blood picture shows macrocytic anemia. (5)
Homocysteine level in blood is increased
Q. What are the sources of folic acid? (Page 278)
A. Yeast, liver, egg, green leafy vegetables, cereals,
and pulses.
Q. What is the daily requirement of folic acid?
(Page 278)
A. The RDA of free folate is 200 mg/day. In pregnancy
the requirement is increased to 400 mg/day.
Q. What is the mechanism of action of sulphona-
mides? (Page 278)
A. They are anti-bacterial agents. They have struc-
tural similarity with PABA. Therefore they com-
petitively inhibit the enzyme responsible for the
incorporation of PABA into folic acid.
Q. What is the mechanism of action of trime-
thoprim? (Page 278)
A. It inhibits the folate reductase and so formation
of THFA is reduced. It is bactericidal agent.
Q. What is mechanism of action of methotrexate?
(Page 278)
A. It inhibits folate reductase, and is a powerful
anticancer drug.
Q. What are inhibitors of folic acid? (Page 278)
A. Methotrexate, trimethoprim, pyrimethamine and
sulphonamide.
Q. Name a water soluble Vitamin, which is stored

in the body.
Q. What is the metal present in Vitamin B12?
(Page 279)
A. Cobalt.
Q. What is the ring system present in Vitamin B 12?
(Page 279)
A. Corrin ring.
Q. Vitamin B12 is absorbed from where?(Page 279)
A. Ileum.
Q. What is the transport form of Vitamin B12?
(Page 279)
A. Methyl B 12.
Q. What is the carrier of Vitamin B12 in blood?
(Page 279)
A. Transcobalamin-II, a glycoprotein, is the specific
carrier.
Q. What is the storage form of Vitamin B12?
(Page 279)
A. It is stored in the liver cells, as ado-B12 form, in
combination with transcobalamin-I or transcorrin.
Q. What is the co-enzyme function of Vitamin B 12?
(Page 279)
A. Methyl malonyl CoA isomerase, and
homocysteine methyl transferase.
Vitamin-II 185
Q. What abnormalities are seen in Vitamin B 12

A. Methyl malonic aciduria, accumulation of methyl
malonic acid, breakdown of myelin sheaths and
interruption in nerve transmission. Homocystein-
uria is also seen.
Q. What abnormal compound is excreted in Vitamin
B12 deficiency?
A. Methyl malonic acid in urine. (Page 280)
Q. What is folate trap? (Page 280)
A. The production of methyl THFA is an irreversible
step. Therefore, the only way for generation of free
THFA is methyl THFA to THFA, by a Vitamin
B12 dependent step. When B12 is deficient, this
reaction cannot take place. This is called the
methyl folate trap.
Q. What is the clinical importance of folate trap?
(Page 280)
A. This leads to the associated folic acid scarcity in
B12 deficiency.
Q. What is the explanation of demyelination in
Vitamin B12 deficiency?
A. In Vitamin B12 deficiency, there is non-avail-
ability of active methionine. Therefore, methyla-
tion of phosphatidyl ethanolamine to phospha-
tidyl choline is not adequate. This leads to
deficient formation of myelin sheaths of nerves.
(Page 280)
Q. What are the causes of B12 deficiency?

(Page 280)
A. Nutritional B12 deficiency, decrease in absorp-
tion, addisonian pernicious anemia, atrophy of
gastric epithelium, and pregnancy.
Q. What is the cause for pernicious anemia?
(Page 280)
A. It is an autoimmune disease with a strong familial
background. Antibodies are generated against
intrinsic factor. So IF is deficient, leading to
defective absorption of B12.
Q. What are the manifestations of Vitamin B12 de-
ficiency? (Page 280)
A. Megaloblastic anemia and subacute combined
degeneration.
Q. What is the difference in folate deficiency and
B12 deficiency?
A. In folate deficiency, there is macrocytic anemia,
and in B12 deficiency, there is additional
neurological symptoms also. (Page 280)
Q. What is the daily requirement of Vitamin B12?
(Page 280)
A. One to two microgram/per day.
Q. A patient who has undergone gastrectomy is
likely to develop deficiency of which Vitamin?
(Page 280)
A. Vitamin B12.
Vitamin-II 187
Q. In Vitamin B12 deficiency, what are the abnorma-

lities seen in urine?
A. Urine may contain methyl malonic acid, homo-
cystine, cystathione, and formimino glutamic acid.
(Page 280)
Q. Which is the Vitamin totally absent in plant
sources?
Q. What are the sources of Vitamin B12?(Page 280)
A. Liver, meat, fish, and curd.
Q. What is the chemical structure of Vitamin C?
(Page 282)
A. L-ascorbic acid.
Q. How it is synthesised? (Page 282)
A. Man and primates cannot synthesise ascorbic
acids. Lower animals could synthesise it from
glucose through glucuronic acid pathway.
Q. What are the major functions of ascorbic acid?
(Page 282)
A. Ascorbic acid promotes collagen formation
through its action on post-translational
hydroxylation of proline and lysine residues.
Q. What are the other functions of ascorbic acid?
(Page 282)
A. Parahydroxy phenyl pyruvate oxidation to homo-
gentisic acid, iron absorption from the intestine,
reconversion of methemoglobin to hemoglobin,
and adrenal steroidogenesis.
Q. Which Vitamin is required for post-translational

modifications?
A. Ascorbic acid. (Page 282)
Q. What is the daily requirement of ascorbic acid?
(Page 283)
A. 75 mg per day.
Q. Scurvy is due to the deficiency of which Vitamin?
(Page 283)
A. Ascorbic acid.
Q. What are the important features of scurvy?
(Page 283)
A. Hemorrhagic tendency, microcytic anemia, bone
pain, bleeding gums.
Mineral Metabolism 189
Mineral Metabolism
Q. What influences absorption of calcium from

intestine? (Page 284)
A. Vitamin D, calcitriol, parathyroid hormone, phytic
acid, and oxalate.
Q. What is the daily requirement of calcium?
(Page 284)
A. 500 mg per day.
Q. What are the sources of calcium? (Page 284)
A. Milk, egg, fish, and vegetables.
Q. What is the function of calcium ? (Page 285)
A. Coagulation, neuromuscular activity, intra-
cellular messenger, activation of enzymes, and
bone formation.
Q. What is the normal level of calcium in blood?
(Page 285)
A. 9-11 mg /dl.
Q. Which will influence serum calcium level?

(Page 285)
A. Calcitriol, calcitonin, and parathyroid hormone.
Q. How parathyroid hormone regulates calcium
level in blood?
A. Bone resorption, increased absorption of calcium
from intestines, and increased absorption of
calcium from renal tubules. (Page 286)
Q. Hypocalcemia results in what clinical condition?
(Page 287)
A. Tetany.
Q. What is the reason for tetany? (Page 287)
A. Hypoparathyroidism.
Q. What are the features of hyperparathyroidism ?
(Page 287)
A. Osteoporosis, hypercalciuria, and urinary calculi.
Q. What is the normal level of phosphorus in blood.
(Page 287)
A. 3-4 mg /dl.
Q. What is the normal level of sodium in blood ?
(Page 289)
A. 136-145 mEq/L.
Q. What is the important extracellular cation?
(Page 289)
A. Sodium.
Q. Which will control the sodium level in serum?
(Page 289)
A. ADH, aldosterone, and cortisone.
Q. What is the normal level of potassium in blood ?

(Page 289)
A. 3.5 to 5 mEq /L.
Q. What is the major intracellular cation?(Page 289)
A. Potassium.
Q. What is the manifestation of hypokalemia?
(Page 289)
A. In ECG, T wave inverted, ST segment is lowered.
Q. What is the normal level of chloride in blood ?
(Page 290)
A. 96- 106 mEq /L.
Q. What is the daily requirement of iron for a
normal adult male ?
A. 10-20 milligram per day. (Page 291)
Q. What are the dietary sources of iron ? (Page 291)
A. Green leafy vegetables, meat, and jaggery.
Q. Which is the trace element, deficient in milk?
(Page 291)
A. Iron.
Q. What are important iron containing proteins?
(Page 291)
A. Hemoglobin, myoglobin, cytochromes, catalase,
tryptophan pyrrolase, xanthine oxidase,
transferrin, and ferritin.
Q. Which will increase iron absorption from
intestines? (Page 291)
A. Gastric HCl, ascrobic acid, and cysteine.
Q. What are the factors which will retard iron

absorption? (Page 291)
A. Phytic acid (in cereals) oxalic acid (in leafy
vegetables), calcium, zinc, lead and phosphates.
Q. Iron is absorbed from which part? (Page 292)
A. Upper part of duodenum.
Q. How is iron absorbed? (Page 292)
A. Iron in the intestinal lumen enters the mucosal
cell in the ferrous state. This is bound to transferrin
molecule present in brush border surface of
intestinal cell. One transferrin molecule can bind
with two atoms of iron. This is then complexed
with a specific receptor. This iron-transferrin-
receptor is internalised.
Q. How iron absorption is regulated? (Page 292)
A. Iron metabolism is unique because homeostasis is
maintained by regulation at the level of absorption
and not by excretion. When iron stores in the body
are depleted, absorption is enhanced. When
adequate quantity of iron is stored, absorption is
decreased. This is referred to as “mucosal block”
of regulation of absorption of iron.
Q. What is the carrier protein in iron in blood?
(Page 292)
A. Transferrin.
Q. Which enzyme will help in iron carriage in
blood? (Page 292)
A. Ferroxidase (ceruloplasmin).
Q. What is the storage form of iron? (Page 293)

A. Ferritin.
Q. What is hemosiderin? (Page 293)
A. Excess iron is loaded as hemosiderin.
Q. What is haptoglobin? (Page 293)
A. It is the carrier of free hemoglobin.
Q. What is hemopexin? (Page 293)
A. It is the carrier of free heme.
Q. Anemia is resulted in the deficiency of which
A. Iron, copper, vitamin C, folic acid, vitamin B12,
and pyridoxal phosphate.
Q. Iron deficiency results in what? (Page 294)
A. Microcytic hypochromic anemia.
Q. What are the features of hemosiderosis?
(Page 294)
A. Cirrhosis of liver, diabetes mellitus, and yellow
colour of skin.
Q. What is the cause for hemosiderosis? (Page 294)
A. Repeated transfusion of whole blood.
Q. What are the important copper containing
enzymes? (Page 294)
A. Ceruloplasmin, cytochrome oxidase, cytochrome
C, tyrosinase, lysyl oxidae, and super oxide
dismutase.
Q. What are dietary sources of copper? (Page 294)
A. Cereals, meat, and liver.
Q. What is ceruloplasmin? (Page 294)

A. It is ferroxidase, and it promotes oxidation of
ferrous ion to ferric form.
Q. What are the characteristic features of Wilson’s
hepatolenticular degeneration? (Page 295)
A. Ceruloplasmin level in blood is decreased, copper
excretion is reduced, and copper is accumulated
in liver to produce cirrhosis.
Q. What is the daily requirement of iodine?
(Page 295)
A. 150-200 microgram.
Q. What is the daily requirement of zinc?
(Page 296)
A. 15-20 milligram.
Q. What are the important enzymes which contain
zinc? (Page 296)
A. Alkaline phosphatase, amylase, carbonic
anhydrase, and RNA polymerase. Zinc is required
for insulin secretion.
Q. What is Fluorosis? (Page 297)
A. It is produced when fluoride concentration in
water is more than 20 ppm. Osteoporosis is the
manifestation.
Q. What is the importance of selenium? (Page 298)
A. It is an anti-oxidant.
Q. Name the selenium containing enzyme.
(Page 298)
A. Glutathione peroxidase.
Energy Metabolism and Nutrition 195
Energy Metabolism
and Nutrition
Q. What is the calorific value of carbohydrates?

(Page 299)
A. Four kilocalories per gram.
Q. What is the calorific value of fats? (Page 299)
A. Nine kilocalories per gram.
Q. How much calories are generated per gram of fat
? (Page 299)
A. kCal.
Q. What is the respiratory quotient? (Page 299)
A. It is the ratio of carbon dioxide produced to the
oxygen consumed.
Q. What is the respiratory quotient of carbohyd-
rates? (Page 299)
A. One.
Q. What is the respiratory quotient for a mixed diet?

(Page 299)
A. About 0.82.
Q. What is specific dynamic action? (Page 300)
A. Increased heat production after intake of food.
Q. Which foodstuff has maximum specific dynamic
action ?
A. Proteins. (Page 300)
Q. Basal metabolic rate is increased in which
A. Fever, starvation, cold climate, and increased
thyroid hormones.
Q. Increased basal metabolic rate is observed in
which clinical condition?
A. Grave’s disease (hyperthyroidism). (Page 300)
Q. What are the beneficial effects of dietary fibre?
(Page 301)
A. Increased motility of intestine, decreased
absorption of cholesterol, and increased glucose
tolerance.
Q. Name an undigestible carbohydrate. (Page 301)
A. Pectin.
Q. Which food stuffs contain polyunsaturated fatty
acids? (Page 302)
A. Vegetable oils, sunflower oil, and groundnut oil.
Q. Name essential fatty acids. (Page 302)

A. Linoleic acid, linolenic acid, and arachidonic acid.
Energy Metabolism and Nutrition 197
Q. What is the dietary advice for a patient with

hypercholesterolemia?
A. They should take polyunsaturated fatty acids.
(Page 302)
Q. What foodstuffs contain cholesterol? (Page 302)
A. Egg, butter, ghee, and pig fat.
Q. A patient with coronary artery disease is advised
to refrain from what?
A. Egg. (Page 302)
Q. What is the recommended daily allowance of
protein of a normal adult? (Page 303)
A. 1 g/kg.
Q. Negative nitrogen balance is observed in which
conditions?
A. Chronic infection, old age, and malnutrition.
(Page 303)
Q. Positive nitrogen balance is observed in which
conditions?
A. Pregnancy, convalescence, and growth period.
(Page 303)
Q. Lysine is deficient in which foodstuff?
(Page 305)
A. Pulses.
Q. Phenyl alanine is deficient in which food stuff?
(Page 305)
A. Tapioca.
Q. Methionine is deficient in which food stuff?
(Page 305)
A. Cereals.
Q. How all amino acids are made available in a mixed

diet?
A. Supplementation by combining cereals and pulses.
(Page 305)
Q. What are the salient features of Kwashiorkor?
(Page 305, 306)
A. Hypoalbuminemia, hypomagnesemia, growth
retardation, lethargy, and loss of appetite.
Q. How much energy is required for a 60 kg person,
with sedentary work?
A. 2000 kCal. (Page 307)
Q. A balanced diet should have calories for
carbohydrate, proteins and fats in which ratio?
(Page 307)
A. 60:20:20.
Detoxification and Biotransformation of Xenobioticsn 199
Acid Base Balance and pH 199
Detoxification and
Biotransformation
of Xenobiotics
Q. What is detoxification process? (Page 310)

A. Biochemical processes whereby noxious
substances are rendered less harmful or more
water soluble and easily excretable.
Q. What are xenobiotics? (Page 310)
A. They are compounds accidentally ingested or
taken as drugs or compounds produced in the
body by bacterial metabolism.
Q. Give an example of a substance detoxified by
reduction. (Page 311)
A. Para nitro phenol.
Q. Give examples of substances detoxified by
hydrolysis. (Page 311)
A. Acetanilide to aniline + acetate, aspirin to salicylic
acid + acetate.
Q. Give names of conjugating agents. (Page 311)

A. PAPS, UDP glucuronic acid, glutathione, and
glycine.
Q. Give some examples of substances detoxified by
conjugation.
A. Bilirubin to bilirubin glucuronide, phenol to
phenyl sulfate, and benzoic acid to hippuric acid.
(Page 311)
Q. Which amino acids are used for detoxification?
(Page 311)
A. Glutamine, glycine, and cysteine.
Q. Give examples of substances detoxified by
sulfation. (Page 311)
A. Phenol to phenyl sulfate, and indole to indoxyl
sulfate.
Q. What is the sulfating agent? (Page 311)
A. PAPS (phospho adenosyl phospho sulfate).
Q. How benzoic acid is detoxified? (Page 311)
A. Benzoic acid + glycine = benzoyl glycine or
hippuric acid.
Q. How epinephrine is excreted? (Page 312)
A. As methyl conjugates.
Q. What is the methylating agent? (Page 312)
A. S-adenosyl methionine.
Biochemical Aspects ofAcid
Environmental
Base BalancePollution
and pH 201
Biochemical
Aspects of
Environmental Pollution
Q. What is the most common environmental

poison? (Page 314)
A. Lead.
Q. What are common causes of lead poisoning?
(Page 314)
A. Paint, lead containig petrol, lead pipes, news-
papers, xerox copies and cigarette smoke are
important contaminants.
Q. What are the occupations in which persons are
prone to get lead poisoning? (Page 314)
A. Battery repair, radiator repair, soldering, paint-
ing and printing.
Q. What is the toxic level of lead? (Page 314)
A. Blood level of lead, more than 10 ?g/dl in children
and more than 25 ?g/dl in adults lead to toxic
manifestations.
Q. What are the manifestations of chronic lead

A. Miscarriage, stillbirth, and premature birth. In
children, mental retardation, learning disabilities,
behavioral problems, hyperexcitability and
seizures are seen. Anemia, abdominal colic and
loss of appetite are very common.
Q. What are the manifestation of acute lead poisoning?
(Page 314)
A. Encephalopathy, convulsions, mania, neuropathy,
abdominal colic, severe anemia and kidney
damage, discolouration and blue line along the
gums.
Q. When does acute toxicity is manifested?
(Page 314)
A. If the blood level of lead is more than 70 mg/dl,
acute toxicity is manifested.
Q. What is the cause of anemia in lead poisoning?
(Page 314)
A. Lead inhibits delta amino levulinic acid (ALA)
synthase, ALA-dehydratase and ferrochelatase.
So, heme synthesis is blocked. Life span of RBC
is shortened. Anemia enhances lead absorption,
lead in turn produces more anemia, thus a vicious
cycle is operating.
Q. What are the antidotes for lead poisoning?
(Page 314)
A. Calcium dodecyl edetate (Calcium disodium
versenate), penicillamine and dimercaprol (BAL)
are used as antidotes. Dimercaptosuccinic acid is
a better but costly antidote.
Acid Base
Balance and pH
Q. What is the pH of 0.1 M hydrochloric acid?

(Page 319)
A. One.
Q. When pH falls by 1 unit, what is the change in
the hydrogen ion concentration? (Page 319)
A. Increases by 10 times.
Q. Relationship between pH and pK is given by
which equation? (Page 320)
A. Henderson-Hasselbalch’s equation.
Q. What determines the pH of buffer? (Page 320)
A. By the ratio of salt to acid.
Q. Buffer is most effective when? (Page 320)
A. When pK of the acid is nearer to pH.
Q. When is the buffering capacity is more?
(Page 320)
A. When the absolute concentrations of salt and acid
are more.
Q. In the blood, which buffer is most effective?

(Page 321)
A. Bicarbonate buffer.
Q. What are the mechanisms for maintaining the
normal pH of plasma? (Page 321)
A. Buffers of plasma, lung mechanism, and kidney
mechanism.
Q. What is the alkali reserve of the body?
(Page 321)
A. Bicarbonate is the alkali reserve.
Q. What is the ratio of bicarbonate to carbonic acid
in blood? (Page 321)
A. Bicarbonate to carbonic acid ratio is 20.
Q. What are the mechanisms by which renal
regulation of acid load is achieved? (Page 323)
A. Excretion of hydrogen ions in urine, excretion of
ammonium ions in urine, and production of
bicarbonate in renal tubules.
Q. Glutaminase enzyme is used for what purpose?
(Page 323)
A. For production of ammonia in kidney tubules.
Q. What is metabolic acidosis? (Page 325)
A. Primary deficit of bicarbonate.
Q. What are the causes of metabolic acidosis?
(Page 326)
A. Diabetic ketosis, chronic renal failure, and
diarrhea.
Q. What are the features of diabetic ketoacidosis?

(Page 326)
A. Lowered bicarbonate, elevated plasma chloride,
and increased anion gap.
Q. What is the formula used to calculate anion gap?
(Page 326)
A. (sodium + potassium) minus (chloride +
bicarbonate).
Q. What is the cause for high anion gap acidosis?
(Page 326)
A. Diabetic ketoacidosis, chronic renal failure, renal
tubular acidosis, lactic acidosis.
Q. What is metabolic alkalosis? (Page 326)
A. Primary excess of bicarbonate.
Q. What are the causes of metabolic alkalosis?
(Page 326)
A. Prolonged vomiting, gastric aspiration, and
ingestion of antacids.
Q. What is respiratory acidosis? (Page 326)
A. Primary excess of carbonic acid.
Q. What are the causes of respiratory acidosis?
(Page 327)
A. Bronchial asthma, bronchopneumonia, and
narcotic poisoning.
Q. What is respiratory alkalosis? (Page 327)
A. Primary deficit of carbonic acid.
Q. What is the cause for respiratory alkalosis?

(Page 327)
A. Hyperventillation.
Q. What are the results of prolonged vomiting?
(Page 327)
A. Alkalosis, hypochloremia, and hypokalemia.
ElectrolyteMolecular
and WaterBiology
BalanceI 207
Electrolyte and
Water Balance
Q. What is the major intracellular cation?(Page 329)

A. Potassium.
Q. What is the major extracellular cation?(Page 329)
A. Sodium.
Q. What is the function of anti diuretic hormone?
(Page 330)
A. Its secretion is stimulated when plasma
osmolarity increases, ADH decreases the urine
output, and retains water in the body.
Q. What are the factors regulating fluid and
electrolyte balance?
A. Aldosterone and anti diuretic hormone.
(Page 330)
Q. What are the diuretic drugs used? (Page 330)
A. Aldosterone antagonists, angiotensin converting
enzyme inhibitors, and carbonic anhydrase
inhibitors.
Q. What is the major cause for isotonic contraction

of ECF? (Page 331)
A. Small intestinal obstruction.
Q. What are the causes for hypotonic contraction of
ECF? (Page 331)
A. Infusion of dextrose (without saline), Addison’s
disease.
Q. What are the causes for hypertonic contraction
of ECF? (Page 331)
A. Diarrhoea, vomiting.
Q. What are the causes for isotonic expansion of
extracellular fluid?
A. Congestive cardiac failure and
hyperaldosteronism. (Page 331)
Q. What is the cause for hypotonic expansion of
extracellular fluid?
A. Inappropriate secretion of ADH. (Page 331)
Q. What is the important cause for hypertonic
expansion of ECF?
A. Cushing’s syndrome. (Page 331)
Q. What are the metabolic imbalances seen in
diarrhea? (Page 331)
A. Metabolic acidosis, hypertonic contraction of ECF,
urine with high specific gravity, and urine output
reduced.
Molecular Biology I 209
Molecular Biology-I:
Nucleotides, Chemistry
and Metabolism
Q. What is a nucleotide? (Page 332)

A. Nitrogenous base + sugar + phosphate.
Q. What is a nucleoside? (Page 332)
A. Nitrogenous base + sugar.
Q. What are the sugars? (Page 332)
A. Ribose in RNA and deoxyribose in DNA.
Q. What are the bases present in nucleotides?
(Page 332)
A. Purines and pyrimidines.
Q. Name the common purines. (Page 332)
A. Adenine and guanine.
Q. Name the common pyrimidines. (Page 332)
A. Cytosine, uracil, and thymine.
Q. What are the bases present in DNA? (Page 332)

A. Adenine, guanine, cytosine, and thymine.
Q. Which nitrogenous base is absent in DNA?
(Page 332)
A. Uracil.
Q. Which base is found exclusively in DNA and not
in RNA? (Page 332)
A. Thymine.
Q. Which base is found exclusively in RNA and not
in DNA? (Page 332)
A. Uracil.
Q. Which amino acid is required for both purine
and pyrimidine synthesis? (Page 333)
A. Aspartic acid and glutamine.
Q. N3 of purine ring is donated by what?(Page 335)
A. Glutamine.
Q. Glycine donates what part of the purine ring?
(Page 335)
A. C4, C5, N7 atoms.
Q. N1 atom of purine ring is coming from what?
(Page 335)
A. Aspartic acid.
Q. One carbon pool donates which carbon atoms
of purine ring?
A. C2 and C8 carbon atoms. (Page 335)
Q. What is the key enzyme of de novo synthesis

pathway of purines? (Page 337)
A. The committed step in de novo synthesis is the
reaction catalysed by amidotransferase (step 1).
Q. How is de novo synthesis of purine regulated?
(Page 337)
A. Amidotransferase enzyme is inhibited by AMP
and GMP.
Q. What are the enzymes needed for salvage
pathway of purines? (Page 337)
A. Adenine phospho ribosyl transferase (APRTase)
and hypoxanthine guanine phospho ribosyl
transferase (HGPRTase).
Q. What is the importance of the salvage pathway?
(Page 337)
A. This is of special importance in tissues like RBCs
and brain where the de novo pathway is not
operating.
Q. What is the clinical significance of the purine
analogues? (Page 338)
A. They act as cell cycle inhibitors and can be used
as anti-cancer drugs.
Q. Give a few examples of purine analogues, used
as anti-cancer drugs. (Page 338)
A. 6-mercapto-purine inhibits the conversion of IMP
to GMP and AMP. 2. Cytosine arabinoside. 3.
Folate antagonists (Methotrexate) would affect the
reactions involving one carbon group transfers.
4. Azaserine is a glutamine antagonist and
therefore inhibits reactions involving glutamine.
Q. What is the end product of catabolism of purines

in human beings?
A. Uric acid. (Page 338)
Q. What is xanthine oxidase? (Page 338)
A. It is the enzyme for the reactions, hypoxanthine
to xanthine and xanthine to uric acid.
Q. What is the speciality in this reaction?(Page 338)
A. Xanthine oxidase is a metalloflavoprotein con-
taining FAD, molybdenum and iron. As xanthine
is oxidised to uric acid, hydrogen peroxide
(reactive oxygen species) is produced.
Q. What is the normal uric acid level in blood?
(Page 338)
A. The normal blood level of uric acid ranges from
2-5 mg/dl in females and 3-7 mg/dl in males.
Q. What is the normal excretion rate of uric acid?
(Page 338)
A. The daily excretion of uric acid varies from 500-
700 mg.
Q. Which property of uric acid is responsible for
the manifestations of gout? (Page 338)
A. Uric acid is sparing soluble in water.
Q. Increased uric acid level is seen in which condi-
tions? (Page 339)
A. Gout, pre-eclampsia, Hodgkin’s lymphoma,
leukemia, and diabetic ketoacidosis.
Q. Hyperuricemia can result from defect of which

enzymes? (Page 339)
A. Ribosyl amido transferase, PRPP synthetase,
HGPRTase, APRTase, Glucose-6-phosphatase,
and glutathione reductase.
Q. Hyperuricemia is observed in which conditions?
(Page 339)
A. Gout, Lesch Nyhan syndrome, von Gierke’s
disease.
Q. What are salient features of Lesch-Nyhan
syndrome? (Page 340)
A. Self mutilation, hyperuricemia, and X-linked
inheritance.
Q. What is the mechanism of action of allopurinol?
(Page 340)
A. It is an analogue of hypoxanthine. It inhibits
xanthine oxidase, and thereby decreasing the
formation of uric acid.
Q. It is what type of inhibition? (Page 340)
A. Xanthine oxidase converts allopurinol to
alloxanthine. It is a more effective inhibitor of
xanthine oxidase. This is a good example of
‘suicide inhibition.
Q. Hypouricemia can result from deficiency of
which enzyme? (Page 340)
A. Adenosine deaminase deficiency.
Q. How is it manifested? (Page 340)
A. Severe immunodeficiency.
Q. What are used for pyrimidine synthesis?

(Page 340)
A. Carbamoyl phosphate and aspartic acid.
Q. What is the rate limiting step in pyrimidine
A. Aspartyl trans carbamoylase.
Q. What is carbamoyl phosphate synthetase II and
how is it different from type I enzyme?
(Page 341)
A. CPS-II is involved in pyrimidine synthesis, but
CPS-I is for urea synthesis. CPS-II is in cytosol,
but CPS-I is in mitochondria. CPS-II is inhibited
by CTP, whereas CPS-I is not.
Q. How is pyrimidine synthesis pathway regulated
in mammals?
A. CPS II is inhibited by CTP. (Page 341)
Q. What is the mechanism of action of 6-mercpto
purine? (Page 342)
A. It inhibits conversion of IMP to AMP, and so acts
as an antimetabolite.
Q. What is the mechanism of action of 5-fluoro
uracil? (Page 342)
A. It inhibits conversion of dUMP to dTTP, and acts
as an antimetabolite.
Q. Orotic aciduria is a feature of deficiency of which
enzymes? (Page 342)
A. OMP decarboxylase, OPRTase, and ornithine
transcarbamoylase.
Q. What are the characteristic features of orotic

aciduria ? (Page 342)
A. Megaloblastic anemia, urinary tract obstruction,
and response to oral uridine therapy.
Q. Formation of dTMP (thymine nucleotide)
requires what enzyme and co-enzymes?
(Page 342)
A. Methylation of dump is done by thymidylate
synthase. The methyl group is donated by
methylene-THFA. Later, THFA is regenerated by
dihydrofolate reductase, using NADPH.
Methotrexate inhibits dihydrofolate reductase
and thereby reduces the regeneration of THFA,
and it is a powerful anticancer agent.
Q. How deoxyribonucleotides are formed?
(Page 342)
A. By the reduction at the 2' carbon of the corres-
ponding nuceloside diphosphates (NDP to
dNDP).
Q. What are the enzymes and co-enzymes for this
reaction? (Page 342)
A. Ribonucleotide reductase, NADPH, and
thioredoxin.
Molecular Biology-II:
DNA structure and Replication
Q. What are the important characteristics of Watson-

Crick model of DNA? (Page 344)
A. Right-handed double helix, each turn of helix has
10 base pairs, Hydrogen bonds between purines
and pyrimidines, and DNA strands running in
opposite directions (anti parallel).
Q. What is base pairing rule? (Page 344)
A. Pairing (hydrogen bonding) of adenine with
thymine and guanine with cytosine. Purine is
paired with pyrimidine A+T = G+C.
Q. What are the modifications seen in histones?
(Page 345)
A. Acetylation, methylation, and phosphorylation.
Q. What is nucleosome? (Page 345)
A. DNA wrapped around histones.
Molecular Biology-III
II 217
Q. What is euchromatin? (Page 346)

A. Transcriptionally active chromatin is called
euchromatin. It is less densely packed, and
sensitive to digestion by DNAse.
Q. What is meant by DNA replication? (Page 346)
A. During cell division, each daughter cell gets an
exact copy of the genetic information of the mother
cell. This process of copying the DNA is known
as DNA replication.
Q. How the exact copying is effected? (Page 346)
A. Each strand serves as a template or mould, over
which a new complementary strand is synthe-
sised. The base pairing rule is always maintained.
Q. What are the enzymes required for DNA
replication? (Page 347)
A. DNA polymerase, topo isomerase, and DNA
ligase.
Q. How many DNA polymerases are there in
mammalian cells?
A. Five. Alpha, beta, gamma, delta, and epsilon.
(Page 347)
Q. What a replisome? (Page 347)
A. DNA replication needs the participation of more
than 20 enzymes and proteins, collectively called
DNA replicase system or replisomes.
Q. What is a replication bubble? (Page 348)
A. Helicases move on both directions, separating the
strands in advance of the replication. This forms
a replication bubble.
Q. Replication is in which direction? (Page 347)

A. Polymerisation of the new strand of DNA is
taking place from 5' to 3' direction. This means
that the template is read in the 3' to 5' direction.
Q. How replication starts? (Page 347)
A. An RNA primer, about 100-200 nucleotides long,
is synthesised by the RNA primase.
Q. What is meant by semiconservative nature of
A. In the daughter cell, one strand is derived from
the mother cell, while the other strand is newly
synthesised. This is called semi-conservative type
of DNA replication.
Q. What is meant by semi-discontinuous nature of
A. DNA synthesis is always in the 5' to 3' direction
in both strands. Replication fork advances
towards one side. So, in one strand, the replication
is taking place continuously, but in the other
strand replication is in small pieces.
Q. What is lagging strand? (Page 348)
A. The strand which is discontinuously synthesised
is referred to as the “lagging strand” and the one
continuously polymerised as the “leading
strand”.
Q. What are okazaki fragments? (Page 348)
A. The small DNA molecules attached to its own
primer RNA in the lagging strand are called
okazaki fragments. The RNA is removed and
DNA pieces are joined by ligases.
Molecular Biology-III
II 219
Q. Xeroderma pigmentosum is due to deficiency of

what process? (Page 349)
A. Defect in DNA repair mechanism (nucleotide
excision repair).
Q. Defect in DNA repair mechanisms produce what
clinical conditions?
A. Xeroderma pigmentosum, ataxia-telangectasia,
Fanconi’s anemia, and Bloom’s syndrome.
(Page 350)
Q. Which enzymes protects cellular ageing?
(Page 350)
A. Telomerase.
Q. In prokaryotes, DNA replication is inhibited by
what drugs?
A. Ciprofloxacine, nalidix acid, and novobiocin.
(Page 350)
Q. DNA replication in eukaryotes is inhibited by
what drugs? (Page 350)
A. 5-fluoro uracil, 6-mercaptopurine, cytosine
arabinoside, and etoposide.
Molecular Biology-III:
Transcription and Translation
Q. What is transcription? (Page 351)

A. The process of making a complementary mRNA
copy of DNA.
Q. The mRNA is a complementary copy of which
strand of DNA?
A. Template strand. (Page 351)
Q. What is coding strand? (Page 351)
A. The opposite strand of template strand. Coding
strand has the same sequence as of the mRNA.
Q. What is the enzyme necessary for the transcrip-
tion? (Page 351)
A. DNA dependent RNA polymerase or RNAP.
Q. What are the different types of RNAP?
(Page 351)
A. RNAP type II or B is the enzyme synthesising
mRNAs. RNAP type I or A is responsible for
synthesis of rRNA while type III or C is
responsible for production of tRNA.
Molecular Biology-III 221
Q. What is the specific inhibitor of RNAP?

(Page 352)
A. RNAP II is inhibited by alpha amanitin.
Q. What is the direction of transcription?(Page 352)
A. It takes place in the 5' to 3' direction.
Q. What is TATA Box? (Page 352)
A. It is a signal for initiation of transcription in
prokaryotes. It is about 10 bp upstream of starting
of mRNA synthesis. It is also called pribnow box.
Q. What is the corresponding signal in mammals?
(Page 352)
A. Godberg-Hogness Box. It is located at -25 to -30
position.
Q. How termination of transcription is effected?
(Page 353)
A. The specific signals are recognised by a termi-
nation protein, the Rho factor, then the RNAP
enzyme dissociates from DNA. There is also Rho
Independent Termination. This is effected by an
interrupted invert repeat in DNA. This is transcri-
bed. So the mRNA makes a hairpin structure. This
obstructs further movement of RNA.
Q. What are post-transcriptional modifications?
(Page 353)
A. Removal of introns, addition of a cap at 5' end,
adding poly A tail at 3' end and methylation.
Q. What are the non-coding sequences? (Page 354)
A. Leader sequence, poly-A tail, introns.
Q. What is intron? (Page 354)
A. Part of mRNA that is removed is called intron.
Q. What is a spliceosome? (Page 354)

A. Small nuclear ribonucleoprotein particles
(SnRNPs) associated with hnRNA at the exon-
intron junction form spliceosomes. This is taking
place inside the nucleus.
Q. What is the cause for systemic lupus erythe-
matosis? (Page 354)
A. Production of auto antibodies against small
nuclear ribonucleoprotein particles cause
systemic lupus erythematosis (SLE), a fatal auto-
immune disease.
Q. What are ribozymes? (Page 354)
A. Enzymes made up of RNA are called ribozymes.
Q. Give some examples of ribozymes. (Page 354)
A. Spliceosomes, RNAse-P (which generates the ends
of tRNAs) and peptidyl transferase (present in
ribosomes) are examples of ribozymes.
Q. Give the names of inhibitors of RNA synthesis.
(Page 354)
A. Rifampicin, actinomycin, mitomycin and amanitin.
Q. What is the mechanism of action of mitomycin?
(Page 354)
A. Actinomycin D and mitomycin intercalate with
DNA strands, thus blocking transcription. They
are used as anticancer drugs.
Q. What is the mechanism of action of Rifampicin?
(Page 354)
A. It binds to beta subunit of RNA polymerase, and
inactivates it. Rifampicin is widely used in the
treatment of tuberculosis and leprosy.
Q. What is the mechanism of action of amanitin?

(Page 354)
A. It inactivates RNA polymerase II.
Q. What is reverse transcriptase? (Page 354)
A. In retroviruses, RNA is the genetic material (not
DNA). The RNA dependent, DNA polymerase or
reverse transcriptase will make a new DNA strand
based on the RNA template. Thus, genetic
information is transferred from RNA to DNA.
Q. Give an example of retrovirus. (Page 355)
A. The human immunodeficiency virus (HIV)
causing AIDS is a retrovirus.
Q. What are the structural features of tRNA
molecule? (Page 355)
A. It has clover shape appearance. It contains unusual
bases. Amino acid binding is at 3' end. The oppo-
site part has anticodon arm.
Q. During protein synthesis, amino acid sequence
is specified by what?
A. The codons present in messenger RNA.
(Page 355)
Q. During replication, DNA is synthesised in which
direction? (Page 356)
A. From 5' to 3' direction.
Q. During transcription, mRNA is synthesised in
which direction?
A. From 5' to 3' direction. (Page 356)
Q. During translation, protein is synthesised in

which direction?
A. From amino terminal end to carboxy terminal end.
(Page 356)
Q. What are the salient features of genetic code?
(Page 356)
A. Triplet codons are consecutive three bases pairs
in mRNA. The codons are non-overlapping,
degenerate, but unambiguous and universal.
Q. What is meant by degeneracy of genetic code?
(Page 356)
A. One amino acid is represented by multiple codons.
Q. What is meant by the term wobbling?(Page 357)
A. Anticodons pair with codons that differ at the
third base.
Q. What is the initiating codon for protein synthesis?
(Page 357)
A. AUG.
Q. What is Shine-Dalgarno sequence? (Page 357)
A. Marker of start signal for translation in bacterial
mRNA.
Q. Where is protein biosynthesis taking place?
(Page 358)
A. Ribosomal assembly either attached to endoplas-
mic reticulum, or in cytoplasm.
Q. How many high energy bonds are required for
the synthesis of one peptide bond? (Page 359)
A. Four high energy bonds.
Q. Give examples of diseases caused by protein

targetting defects.
A. Zellweger syndrome, adrenoleukodystrophy and
primary hyperoxaluria. (Page 360)
Q. What is the function of signal peptide?
(Page 360)
A. Causes anchorage of ribosome to endoplasmic
reticulum, and so directs the new protein into the
endoplasmic reticulum. Such proteins are des-
tined for secretion.
Q. What is the location of signal peptide?
(Page 360)
A. In the amino terminal region of the nascent protein.
Q. What is the location of the address for destination
of proteins?
A. These are in the carboxy terminal end of proteins.
(Page 360)
Q. Give examples for post-translational modifications.
(Page 361)
A. Gamma carboxylation of prothrombin, hydroxy-
lation of proline in collagen, methylation of
histones, and glycosylation of proteins.
Q. Give examples of diseases produced by defect
in post-translational modifications. (Page 361)
A. Lathyrism, Ehlers-Danlos syndrome, and scurvy.
Q. Give examples of inhibitors of translation in
eukaryotic cells?
A. Puromycin, cycloheximide, diphtheria toxin, and
ricin. (Page 361)
Q. What is the mechanism of action of erythromycin?

(Page 361)
A. Inhibition of translocation in prokaryotes.
Q. What is the mechanism of action of tetracycline?
(Page 361)
A. Inhibition of tRNA binding to ribosome in bacteria.
Q. What is the mechanism of action of streptomycin?
(Page 361)
A. Misreading of codes and inhibition of initiation
complex formation in bacteria.
Q. What is the mechanism of action of chloram-
phenicol? (Page 361)
A. Inhibition of peptidyl transferase in bacteria.
Q. Give examples of reversible inhibitors of protein
synthesis in bacteria.
A. These antibiotics are bacteriostatic. Tetracyclins,
chloramphenicol, erythromycin and clindamycin
are examples. (Page 361)
Q. Give an example of irreversible inhibitor of pro-
tein synthesis in bacteria. (Page 361)
A. These antibiotics are bactericidal. Streptomycin
is an example.
Q. Leber’s hereditary optic neuropathy is due to
what? (Page 362)
A. Due to mutation in mitochondrial DNA.
MolecularBiology-IV
Molecular Biology-V 227
Molecular Biology-IV:
Molecular Genetics and
Control of Gene Expression
Q. Give examples of X-chromosome linked trans-

mission. (Page 364)
A. Hemophilia, glucose-6-phsophate dehydrogenase
deficiency, and duchenne type muscular dystrophy.
Q. What is a mutation? (Page 366)

A. An alteration in the genetic material results in a
mutation.
Q. Give an example. (Page 366)
A. HbS or sickle-cell hemoglobin is produced by a
mutation of the beta chain in which the 6th position
is changed to valine, instead of the normal
glutamate.
Q. What type of mutation is it? (Page 366)
A. Here, the normal codon GAG is changed to GUG
(transversion).
Q. Give an example for an unacceptable mutation.

(Page 366)
A. Haemoglobin M.
Q. Give examples for mutagens. (Page 367)
A. Acridine orange, X-rays, gamma rays, and methyl
cholanthrene.
Q. How mutagenecity of a compound is tested?
(Page 367)
A. By Ame’s test.
Q. In which phase of the cell cycle, DNA synthesis
is maximum?
A. S phase. (Page 368)
Q. What is the p53? (Page 368)
A. It is an oncosuppressor gene product.
Q. Give examples of enzyme induction. (Page 370)
A. Beta galactosidase by lactose, tryptophan
pyrrolase by glucocorticoid and ALA synthase by
barbiturates.
Q. Give an example of repression. (Page 370)
A. ALA synthase by heme.
Q. Give names of some important antiviral drugs.
(Page 371)
A. Acyclovir, Ribavirin, Zidovudine.
Q. What is a prion? (Page 372)
A. “Prions” is the acronym for “proteinaceous
infective particles”.
Molecular Biology-V:
Recombinant DNA
Technology and Gene Therapy
Q. What are the uses of recombinant DNA

technology? (Page 374)
A. Quantitative preparation of bio-molecules,
especially human proteins. Risk of contamination
is eliminated, when preparing such biomolecules.
Specific probes for diagnosis of diseases can be
prepared. It is used in gene therapy.
Q. What are restriction endonucleases? (Page 374)
A. Restriction endonucleases are referred to as
“molecular scissors”. These enzymes recognise
specific sequence with palindrome arrangement
in the double stranded DNA, and then cleave at
those sites. They are useful in recombinant DNA
technology.
Q. What are required for preparing a recombinant
DNA molecule?
A. Restriction endonuclease, plasmid vector, and
DNA ligase. (Page 375)
Q. How are DNA fragments separated? (Page 378)

A. Agarose gel electrophoresis.
Q. What is Southern blotting? (Page 378)
A. DNA is isolated, fragmented by restriction
endonucleases, cut pieces are electrophoresed in
agarose gel, then blotted over to a nitrocellulose
membrane, when single-stranded DNA will be
adsorbed in the nitrocellulose membrane. The
radio active probe is placed over the membrane.
The membrane is then thoroughly washed and
autoradiographed.
Q. What is the use of Southern blotting?(Page 378)
A. To identify abnormal genes, to demonstrate virus
integration, prenatal diagnosis.
Q. Give some examples of genetic diseases that
could be identified by Southern blotting.
(Page 379)
A. Sickle cell anemia, Huntington’s chorea,
Duchenne muscular dystrophy.
Q. What is Northern blotting? (Page 379)
A. The Northern blot is used to demonstrate specific
RNA.
Q. What is Western blotting? (Page 379)
A. In this technique, proteins (not nucleic acids) are
identified. The proteins are isolated from the
tissue and electrophoresis is done. The separated
proteins are then transferred on to a nitrocellulose
membrane. After fixation, it is probed with
radioactive antibody and auto-radiographed.
Q. What is meant by the term cloning? (Page 379)

A. The term cloning has two broad meanings. When
a gene of higher organism is introduced into a
bacterial DNA, it is called “cloning of the gene”
or “molecular cloning”. When a cell from an
animal is grown to an exact duplicate of that
animal, it is known as “cloning of an animal” or
“somatic cloning”.
Q. What are the applications of cloning of animals?
(Page 379)
A. Animals with genetically desirable traits could be
bred more efficiently, e.g. cows yielding more
milk. Cows or goats may be genetically engineered
to produce milk containing any human protein.
Q. RFLP (restriction fragment length polymorp-
hism) is used for what?
A. Locating mutations in DNA. (Page 381)
Q. What is the application of DNA fingerprinting?
(Page 381)
A. It has medico-legal application.
Q. What are the vectors used for gene therapy?
(Page 381)
A. Retrovirus, adenovirus, and plasmid liposome
complex.
Q. Give some diseases in which gene therapy is
used successfully?
A. Severe combined immuno deficiency, duchenne
muscular dystrophy, cystic fibrosis, familial
hypercholesterolemia, and hemophilia.(Page 382)
Q. What is transgenesis? (Page 383)

A. It is a form of germ cell gene therapy. A
recombinant DNA segment, containing the
desired gene from another species, is introduced
into the fertilized ova. The embryos are allowed
to develop in the uterus of another animal.
Q. What is the technique used for gene amplifi-
cation? (Page 384)
A. Polymerase chain reaction.
Q. Which enzyme is required for PCR (polymerase
chain reaction)?
A. Taq polymerase. (Page 384)
Q. What is reverse PCR? (Page 384)
A. This allows cDNA synthesis from mRNA
followed by PCR amplification. In ordinary PCR,
DNA is detected, that DNA could be from a living
or non-living organism. But in reverse PCR,
mRNA is detected, that means, it is derived from
a living organism.
Q. What is the use of PCR? (Page 384)
A. Diagnosis of bacterial and viral diseases,
medicolegal cases, diagnosis of genetic disorders,
especially prenatal diagnosis. Only very minute
quantity of sample is required.
Clinical
Biochemistry
Biochemistry-III
of AIDS 233
233
Biochemistry of AIDS
Q. What is the full form of AIDS? (Page 387)

A. Acquired immuno deficiency syndrome.
Q. What is the causative organism of AIDS?
(Page 387)
A. Human immunodeficiency virus.
Q. How can you detect window period of the
disease? (Page 387)
A. In the window period viral capsid antigen (p24)
can be detected
Q. What are the usual laboratory findings in the
diagnosis of AIDS?
A. The antibodies against gp120 are detected by the
ELISA test. To rule out the false positive test, the
ELISA positive blood, is then retested with
Western blot analysis. (Page 388)
Q. What other special tests could be done?

(Page 388)
A. T-helper cell count is below 300/ cu.mm. By
RTPCR (reverse transcriptase polymerase chain
reaction, the number of HIV particles in blood can
be estimated, a value of less than 5000 copies per
ml of blood has good prognosis, while a count
more than 1 lakh per ml means very bad prognosis.
Q. HIV belongs to which group of virus?(Page 388)
A. It is a retrovirus. It is an RNA virus.
Q. What is the characteristic of retrovirus?
(Page 388)
A. It contains the enzyme reverse transcriptase.
Q. How the virus gets entry into the tissue cells?
(Page 388)
A. The gp 120 of the virus envelope will specifically
bind with CD4 molecules on the surface of target
cells. CD4 acts as a receptor for the virus.
Q. Where is CD4 molecules present? (Page 388)
A. The CD4 molecules are present on the surface of
T-helper cells.
Q. What are the major groups of anti-HIV drugs
available? (Page 390)
A. Reverse Transcriptase (RT) inhibitors and
protease inhibitors.
Q. How RT inhibitors are classified? (Page 390)
A. nucleoside analogues, non-nucleoside analogues
and nucleotide analogues.
Clinical
Biochemistry
Biochemistry-III
of Cancer 235
235
Biochemistry of Cancer
Q. Name some chemical carcinogens. (Page 391)

A. Methyl cholanthrene, aflatoxins, benzopyrenes.
Q. Name some physical carcinogens. (Page 393)
A. X-ray, gamma-ray and UV-ray.
Q. Name some anti-mutagens and anti-carcinogens.
(Page 393)
A. Vitamin A, Vitamin C, Vitamin E, and curcumin.
Q. Name some oncogenic viruses. (Page 393)
A. Epstein Barr virus (EBV), hepatitis B virus(HBV),
and human papilloma virus.
Q. What are Oncogenes? (Page 394)
A. Genes capable of causing cancer. Oncogenes are
specific sequences in DNA which when expressed
may produce cancer.
Q. What are proto-oncogenes? (Page 394)
A. Oncogenes present in normal cells are also called
as proto-oncogenes.
Q. Proto-Oncogenes may be activated by what

mechanisms? (Page 395)
A. Viral infection, mutation in proto-oncogene,
promoter insertion, and chromosome translocation.
Q. Name a cancer, produced by the deletion of an
oncosuppressor gene?
A. Retinoblastoma. (Page 396)
Q. What are tumour markers? (Page 398)
A. They are factors released from the tumour cells,
which could be detected in blood and therefore
indicate the presence of the tumour in the body.
Q. What is the clinical application of tumour
markers? (Page 398)
A. They are useful for the following purposes. (1)
For follow up of cancer and to monitor the
effectiveness of the therapy. (2) To detect the
recurrence of the tumour
Q. Name some important tumour markers.
(Page 399)
A. Alpha feto protein, carcino embryonic antigen,
prostate specific antigen, neuron specific enolase,
beta chain of human chorionic gonadotropin, and
regan iso-enzyme of alkaline phosphatase.
Q. Alpha feto protein (AFP) level in serum is
increased in which condition?
A. Hepatoma. (Page 399)
Q. Carcino embryonic antigen level is increased in
which type of cancers? (Page 399)
A. Colorectal and gastrointestinal cancers.
Clinical
Biochemistry
Biochemistry-III
of Cancer 237
237
Q. What is the significance of beta chain of human

chorionic gonadotropin? (Page 399)
A. It is a tumour marker for choriocarcinoma.
Q. What is the mechanism of action of mitomycin?
(Page 400)
A. Intercalation with DNA strands.
Q. What is the mechanism of action of Methotrexate?
(Page 400)
A. It is a folic acid antagonist.
Q. What is vincristine and vinblastine? (Page 400)
A. They are alkaloids from vinca rosea, they interfere
with assembly of cytoskeleton and inhibits stath-
mokinesis (spindle movement), so they are used
as anti-cancer drug.
Q. What is the mechanism of action of adriamycin?
(Page 400)
A. It inhibits topo-isomerase.
Applications of
Radio-isotopes
in Medicine
Q. What is an Isotope?
A. Isotopes of a given element will have different
atomic weights, but will have same atomic
number.
Q. Radiation hazard is mainly due to which type of
radiation?
A. Alpha radiation.
Q. Iodine-125 emits mainly emits which type of
radiation?
A. Gamma radiation.
Q. What is the isotope used for DNA studies?
A. P-32.
Q. P-32 is used clinically for what purpose?
A. To treat polycythemia vera.
Applications of Radio-isotopes in Medicine
Clinical Biochemistry-III 239
239
Q. Which radio-active compound is used to measure

glomerular filtration rate (GFR)?
A. 131-Iodine labelled hippuran.
Q. For RIA (radio immuno assay), the radio-active
isotope used is:
A. 125-Iodine.
Q. What is the use of radio active radium in
medicine?
A. Intracavity application of radiation, such as
carcinoma cervix or body of uterus.
Q. What is the common source of radiation in
teletherapy?
A. 137-Cs (caesium) with a half-life of 30 years.
Q. What are radiosensitive tumours?
A. Lymphomas, Hodgkin’s disease and neuroblas-
toma are highly radiosensitive.
Q. What are the important toxic effects of radiation?
A. Leukopenia, thrombocytopenia, and radiation
dermatitis.
Body Fluids
Q. How lactose is synthesised? (Page 407)

A. UDP glucose is epimerased to UDP galactose.
Then the galactose unit is transferred from UDP-
galactose to glucose. This synthesis of lactose in
mammary gland is catalysed by lactose synthase.
Q. How lactose synthesis is regulated? (Page 407)
A. The lactose synthase has two subunits, a catalytic
subunit which is a galactosyl transferase and a
modifier subunit that is alpha lactalbumin. The
level of the modifier subunit is under the control
of prolactin.
Q. What is the major difference between human
and cow’s milk?
A. Human milk has higher carbohydrate content than
cow’s milk while protein content is less.
(Page 407)
Q. How is to humanize cow’s milk? (Page 407)
A. To humanise cow’s milk, protein is to be diluted
and carbohydrate is to be added. Thus, to one cup
of cow’s milk, add half a cup of water and two
teaspoons of sugar. This will make it comparable
to human milk.
Body Fluid
241
Q. Milk contains which type of fatty acids?

(Page 407)
A. The fatty acids are mainly saturated, but 50% of
them are medium chain fatty acids (Lauric and
Myristic acids).
Q. What is the advantage of medium chain fatty
acids? (Page 407)
A. They are easily digested, absorbed and
metabolized.
Q. What is the major protein in cow’s milk?
(Page 407)
A. Eighty percent protein of cow’s milk is casein.
Q. What type of protein is casein? (Page 407)
A. It is a phospho-protein.
Q. How the phosphate group is attached to protein?
(Page 407)
A. The phosphate groups are added to the hydroxyl
groups of serine or threonine residues.
Q. What is whey? (Page 407)
A. If milk is acidified and pH lowered to 4.7, the
casein is precipitated (iso-electric precipitation).
The supernatant is called whey.
Q. What are the proteins present in whey?
(Page 407)
A. Lactalbumin, lactoglobulin and lysozyme.
Hormones-I:
Mechanism of
Action of Hormones
Q. What are G proteins? (Page 410)

A. They are involved in signal transduction.
Q. How the G proteins work? (Page 410)
A. The receptors are in membrane, and binding of
hormone causes activation of G protein.
Q. How is G protein activated? (Page 411)
A. Binding of hormone on receptor causes
attachment of GTP to G protein, and thereby G
protein is activated.
Q. What is the function of activated G protein?
(Page 411)
A. Activated G protein activates adenyl cyclase.
Q. What is the function of adenyl cyclase?
(Page 411)
A. Adenyl cyclase will produce cyclic AMP.
Q. How adenyl cyclase is destroyed? (Page 411)
A. By phospho diesterase.
Hormones-I
243
Q. How cyclic AMP further works? (Page 411)

A. Cyclic AMP activates protein kinase.
Q. What is the function of protein kinase?
(Page 411)
A. It phosphorylates enzymes or target proteins, so
that they are activated.
Q. Name some hormones which act through cyclic
AMP as the second messenger. (Page 410)
A. Glucagon, ACTH, TSH, ADH, FSH, LH.
Q. Name some second messengers. (Page 412)
A. Cyclic AMP, 1,2-diacyl glycerol, inositol
triphosphate, and calcium.
Q. Name some hormones which act through cyclic
GMP as the second messenger. (Page 410)
A. ANF (atrial natriuretic factor).
Q. Name some hormones that bind to intracellular
receptors. (Page 413)
A. Glucocorticoids, mineralocorticoids, estrogens,
progesterone, androgens, and thyroxin.
Hormones-II:
Pituitary Hormones
Q. What are hypothalamic neuropeptides?

(Page 414)
A. These neurohormones are antidiuretic hormone
(ADH) and oxytocin.
Q. Name the important hypothalamic releasing factors.
(Page 415)
A. TRH (thyrotropin releasing hormone), GnRH
(gonadotropin releasing hormone), GHRH
(growth hormone releasing hormone),
somatostatin (growth hormone inhibitory factor),
CRF (corticotropin releasing factor), and PIF
(prolactin inhibitor factor).
Q. Alpha chain of human chorionic gonadotropin
(HCG) is shared with what else? (Page 415)
A. TSH, FSH, LH and HCG have the common alpha
chain, and beta chains are specific.
Hormones-II
245
Q. What are the hormones produced by anterior

pituitary? (Page 415)
A. GH (Growth hormone), ACTH (Adrenocorti-
cotropic hormone), LH (Luteinising hormone),
FSH (Follicle stimulating hormone), TSH (Thyroid
stimulating hormone), MSH (Melanocyte
stimulating hormone), and PRL (Prolactin).
Q. What is the major effect of growth hormone?
(Page 415)
A. GH increases the uptake of amino acids by cells,
enhances protein synthesis, and produces positive
nitrogen balance. The anti-insulin effect of GH
causes lipolysis and hyperglycemia. The overall
effect of GH is to stimulate growth of soft tissues,
cartilage and bone. It is anabolic.
Q. Increased secretion of growth hormone will lead
to what condition?
A. Excess secretion of GH secretion leads to
gigantism in children and acromegaly in adults.
(Page 415)
Q. What is the result of decreased growth hormone
secretion? (Page 415)
A. Deficiency of GH secretion in early childhood
results in pituitary dwarfism.
Q. What is the function of FSH? (Page 416)
A. FSH stimulates growth of ovarian follicles in females
and spermatogenesis (Sertoli cells) in males.
Q. What is the function of LH? (Page 416)
A. Testosterone in males (secreted by Leydig
interstitial cells) and progesterone in females
(secreted by corpus luteum), are increased under
the influence of LH.
Hormones-III:
Steroid Hormones
Q. The 11-hydroxylase is required for the synthesis

of which hormone?
A. Cortisol. (Page 417)
Q. The 17-hydroxylase is required for the synthesis
of which hormones?
A. Cortisol, testosterone, and estradiol.
(Page 417 and 418)
Q. Which is the precursor of steroid hormones?
A. Cholesterol. (Page 417)
Q. What are the hormones produced from
progesterone? (Page 417)
A. Corticosterone, aldosterone, testosterone, and
estrogens.
Q. Cortisol has how many carbon atoms?(Page 417)
A. 21.
Q. Aldosterone has how many carbon atoms?
(Page 418)
A. 21.
Clinical Biochemistry-III
Hormones-III 247
246
Q. Testerone has how many carbon atoms?

(Page 418)
A. 19.
Q. Estrogen has how many carbon atoms?
(Page 418)
A. 18.
Q. What is the immediate precursor of estrogens?
(Page 418)
A. Testosterone.
Q. What are the structural features of estradiol?
(Page 418)
A. Cyclopentanophenanthrene ring, total 18 carbon
atoms, aromatic character of A ring, and hydroxyl
groups on 3rd and 17 carbon atoms.
Q. 21-hydroxylase is required for the synthesis of
which hormone?
A. Aldosterone. (Page 418)
Q. What are the effects of glucocorticoids?
(Page 419)
A. Increased gluconeogenesis, augmented lipolysis,
elevated protein breakdown, and depressed
immune function
Hormones-IV:
Thyroid Hormones
Q. What is the precursor of thyroxin? (Page 423)

A. Tyrosine.
Q. Name some antithyroid agents. (Page 423)
A. Thiocyanate, perchlorate, and methimazole.
Q. How thyroid hormones are produced?(Page 423)
A. Tyrosine residues of thyroglobulin are iodinated.
Q. What is the function of thyroid stimulating
hormone? (Page 423)
A. It increases the uptake of iodine by thyroid gland,
enhances the oxidation of iodine to iodide, and
favours the hydrolysis of thyroglobulin to
produce T4.
Q. What is the ratio of T4 and T3 in blood?
(Page 424)
A. Blood concentration of T4 is 70 times more than
of T3.
Clinical Biochemistry-III
Hormones-IV 249
249
Q. What are the functions of thyroid hormones?

(Page 424)
A. Calorigenic effect or thermogenesis and BMR is
increased.
Q. How this is produced? (Page 424)
A. The thermogenic effect is mediated by uncoupling
of oxidative phosphorylation. Thyroxine in large
quantities can swell the mitochondria. Basal
metabolic rate (BMR) is increased.
Q. What are the biochemical features of thyroid
hormones? (Page 424)
A. Thyroxine increases cellular metabolism.
Gluconeogenesis and carbohydrate oxidation are
increased. Glucose tolerance test shows rapid
absorption. Fatty acid metabolism is increased.
Q. Deficiency of thyroxine results in which
A. Myxedema.
Q. What are the salient features of hypothyroidism?
(Page 426)
A. Decreased T3 level, increased TSH level, lethargy,
hypercholesterolemia, weight gain, and decreased
basal metabolic rate.
Q. What are the characteristic features of primary
hyperthyroidism?
A. High TSH and T4 levels, increased rate of
metabolism, weight loss, tachycardia, fine tremors,
sweating, diarrhea, emotional disturbances, anxiety
and sensitivity to heat. (Page 426)
Clinical Biochemistry-I
Q. Why sodium fluoride is used as a preservative

of blood for glucose estimation? (Page 427)
A. To prevent glycolysis and to prevent loss of sugar.
Q. What are the preservatives used in urine sample?
(Page 427)
A. Formalin, thymol, chloroform, toluene,
concentrated HCl and glacial acetic acid are the
commonly used urine preservatives.
Q. What is optical density? (Page 428)
A. Optical density = minus logT.
Q. What is Beer-Lambert’s law? (Page 428)
A. As per Beer’s law, the intensity of the colour is
directly proportional to the concentration of the
coloured particles in the solution. The Lambert’s
law states that the amount of light absorbed by a
coloured solution depends on the length of the
column or the depth of the liquid through which
light passes.
Clinical
Clinical
Biochemistry-III
Biochemistry-I 251
Q. What is end point analysis? (Page 428)

A. Serum sample and reagents are mixed and
incubated for a fixed time, to develop the colour
optimally. Then, the OD is ascertained and the
concentration of the substances is calculated. This
is called end point analysis.
Q. What is kinetic method? (Page 429)
A. Serum and reagents are incubated, and readings
are taken at 2 and 3 minutes exactly, and from the
difference in OD between the two values, the
concentration is calculated. Here the optimum
colour is not developed, but is quicker and hence
is often used in autoanalysers.
Q. What is accuracy? (Page 430)
A. Accuracy is the closeness of a result to the true
value.
Q. What is meant by the term precision? (Page 430)
A. Precision refers to the reproducibility of the result.
Precision depends on the technique, the reagents,
as well as on the technician.
Q. What is meant by specificity? (Page 430)
A. Specificity of a reaction denotes that only one
substance will answer that particular test.
Specificity is determined by the method of the
analysis.
Clinical Biochemistry-II:
Liver and Gastric Function Tests
Q. What is the normal serum bilirubin level?

(Page 431)
A. 0.2 to 0.8 mg/dl.
Q. What is the normal blood level of unconjugated
bilirubin? (Page 431)
A. 0.2-0.6 mg/dl.
Q. What is the normal serum level of conjugated
bilirubin? (Page 431)
A. Less than 0.2 mg/dl.
Q. What is latent jaundice? (Page 431)
A. Serum bilirubin between 1 mg/dl and 2 mg/dl.
Q. Jaundice appears at what level of bilirubin?
(Page 431)
A. Jaundice appears if the serum bilirubin goes above
2 mg/dl.
Clinical
ClinicalBiochemistry-III
Biochemistry-II 253
Q. What is meant by van den Bergh’s direct positive

test? (Page 431)
A. When bilirubin is conjugated, the purple colour
is produced immediately on mixing with the
reagent, the response is said to be van den Bergh’s
direct positive.
Q. What is indirect positive van den Bergh’s test?
(Page 431)
A. When the bilirubin is unconjugated, the colour is
obtained only when alcohol is added, and this
response is known as indirect positive.
Q. What type of bilirubin is present in hemolytic
jaundice? (Page 431)
A. In hemolytic jaundice, unconjugated bilirubin is
increased in serum. Hence van den Bergh’s test is
indirect positive.
Q. What happens in obstructive jaundice?
(Page 431)
A. In obstructive jaundice, conjugated bilirubin in
serum is elevated, and van den Bergh’s test is
direct positive.
Q. What about hepatocellular jaundice? (Page 431)
A. In hepatocellular jaundice, a biphasic reaction is
observed, because both conjugated and unconju-
gated bilirubins are increased in serum.
Q. What are important liver function tests?
(Page 432)
A. Serum bilirubin, albumin, alkaline phosphatase,
urine bile salts, bile pigments and urobilinogen.
Q. Increase in serum unconjugated bilirubin occurs

in which condition?
A. Hemolytic jaundice. (Page 433)
Q. What are the features of obstructive jaundice?
(Page 433)
A. Elevated conjugated bilirubin in plasma, presence
of bile salts and bile pigments in urine, increased
alkaline phosphatase level in blood, and increased
cholesterol in blood.
Q. Which tests will be positive in a urine of a patient
with obstructive jaundice? (Page 433)
A. Gmelin’s test, Hay’s test, and Fouchet’s test.
Q. What are the enzymes useful in diagnosis of liver
diseases? (Page 433)
A. Alanine amino transferase, alkaline phosphatase,
and gamma glutamyl transferase.
Q. What are the salient laboratory findings in a
patient with chronic liver disease? (Page 433)
A. Serum albumin is lowered, albumin globulin ratio
is reversed, and prothrombin time is prolonged.
Q. What is the characteristic laboratory findings in
alcoholic cirrhosis?
A. Elevation of gamma glutamyl transferase level in
serum. (Page 433)
Q. What are the important stimulants for gastric acid
secretion?
A. Gastrin, vagus stimulation, and histamine.
(Page 434)
ClinicalBiochemistry-III
Clinical Biochemistry-II 255
Q. What is alkaline tide? (Page 434)

A. When HCl is produced in stomach, bicarbonate
level within the cell increases (formed from
H2CO3), it is reabsorbed into blood stream. This
would account for the alkaline tide of plasma and
urine, immediately after meals.
Q. What is the maximal gastric acid output?
(Page 435)
A. It is the acid output in millimol per hour, after
the stimulation.
Q. What is the upper limit of maximal gastric acid
output? (Page 435)
A. 30 mmol/ hour in females and 45 mmol/hour in
males.
Q. What is basal acid output? (Page 435)
A. It is the acid output in millimol per hour, in the
absence of all intentional stimulation.
Q. What is the upper limit of basic acid output?
(Page 435)
A. 5 millimol/hour in females and 10 millimol in
males.
Q. Hypo-acidity is found in which conditions?
(Page 435)
A. Pernicious anemia, carcinoma of stomach, and
atrophic gastritis.
Clinical
Biochemistry-III:
Kidney Function Tests
Q. How much is glomerular filtration rate?

(Page 436)
A. 120-125 ml per minute.
Q. What is the function of glomerulus? (Page 436)
A. An ultrafiltrate of the blood is produced in
glomerulus, while the cells and proteins are
retained in the blood.
Q. What is the normal renal threshold value for
glucose? (Page 437)
A. Blood level of 180 mg/ dl.
Q. What is the normal specific gravity of urine?
(Page 438)
A. 1.015 to 1.025.
Q. What is the minimum and maximum specific
gravity of urine?
A. 1.003 to 1.032. (Page 438)
Q. What is the specific gravity of urine in chronic

renal failure?
A. Fixed to 1.010. (Page 439)
Q. Specific gravity of urine increased in which
A. Acute glomerulonephritis.
Q. Polyuria is seen in which conditions?(Page 439)
A. Diabetes mellitus, diabetes insipidus, and chronic
renal failure.
Q. What are the features of chronic renal failure?
(Page 439)
A. Urine with fixed specific gravity of 1.010, polyuria,
increased blood urea and creatinine.
Q. Name abnormal substances seen in urine.
(Page 439)
A. Protein, blood, sugar, ketone bodies, bile salts,
bile pigments, and urobilinogen.
Q. Proteinuria is seen in which conditions?
(Page 439)
A. Acute glomerulo nephritis, nephrotic syndrome,
pyelonephritis, and multiple myeloma
Q. Which test is commonly employed to detect
urinary protein?
A. Heat and acetic acid test. (Page 439)
Q. What is micro-albuminuria? (Page 439)
A. When small quantities of albumin (50-300 mg/
day) is seen in urine.
Q. How proteinurias are classified? (Page 439)

A. Glomerular proteinuria, overflow proteinuria,
nephron loss proteinuria, tubular proteinuria, and
urogenic proteinuria.
Q. What is meant by renal clearance? (Page 441)
A. Clearance is defined as the quantity of blood or
plasma completely cleared of a substance per unit
time and is expressed as milliliter per minute. It
is the ml of plasma which contains the amount of
that substance excreted by the kidney within a
minute.
Q. How renal plasma flow is measured? (Page 441)
A. Para amino hippurate (Diodrast) clearance.
Q. What is the correct method for assessing
glomerular filtration rate?
A. Inulin clearance. (Page 441)
Q. What is its disadvantage? (Page 441)
A. Inulin has to be infused intravenously throughout
the test period.
Q. What is the normal value for PAH clearance ?
(Page 442)
A. About 700 ml/min.
Q. What is the best method for assessing glomerular
filtration rate?
A. Creatinine clearance test. (Page 442)
Q. What is the advantage of creatinine test?
(Page 442)
A. Creatinine is formed spontaneously (non-
enzymatic), so the blood level and excretion rate
of creatinine is a constant from day to day.
Q. What is the normal value of creatinine clearance?

(Page 442)
A. In males 85-125 ml/min and in females 80-115 ml/
min.
Q. What is the significance of creatinine clearance?
(Page 442)
A. A decreased creatinine clearance is a very
sensitive indicator of a reduced glomerular
filtration rate.
Q. What is the normal creatinine level in blood?
(Page 442)
A. For adult males, 0.7-1.4 mg/dl, for adult females,
0.6-1.3 mg/dl.
Q. What is creatinine coefficient? (Page 442)
A. It is the urinary creatinine expressed in mg/kg
body weight.
Q. What is the significance of creatinine coefficient?
(Page 442)
A. The value is elevated in muscular dystrophy.
Q. What is the normal value of creatinine coefficient?
(Page 442)
A. Normal range is 20-28 mg/kg for males and 15-
21 mg/kg for females.
Q. Urea clearance is lowered in which condition?
(Page 443)
A. Chronic liver failure.
Q. What is the maximum urea clearance value?
(Page 443)
A. 75 ml/minute.
Q. What is the standard urea clearance value?

(Page 443)
A. 54 ml/minute.
Q. When do you call it standard urea clearance?
(Page 443)
A. When the volume of urine formed is less than 2
ml per minute.
Q. What is the normal blood urea level? (Page 443)
A. 20-40 mg /dl.
Q. What is the clinical significance of increased urea
level in blood ?
A. Urea level is increased in renal failure.(Page 443)
Q. How failure of concentrating capacity of urine is
measured ?
A. Concentration test (Water deprivation test).
(Page 444)
Q. How is tubular concentrating capacity measured?
(Page 444)
A. Urine specific gravity.
Q. What are the usual tests to assess tubular
function? (Page 444)
A. Measurement of specific gravity, concentration
test, dilution test, acidification test.
Published by
Jitendar P Vij
Jaypee Brothers Medical Publishers (P) Ltd
EMCA House, 23/23B Ansari Road, Daryaganj
New Delhi 110 002, India
Phones: 3272143, 3272703, 3282021, 3245672, 3245683 Fax: 011-3276490
e-mail: jpmedpub@del2.vsnl.net.in
Visit our web site: http://www.jpbros.20m.com
Branches
• 202 Batavia Chambers, 8 Kumara Kruppa Road, Kumara Park East,
Bangalore 560 001, Phones: 2285971, 2382956 Tele Fax: 2281761
e-mail: jaypeebc@bgl.vsnl.net.in
• 282 IIIrd Floor, Khaleel Shirazi Estate, Fountain Plaza
Pantheon Road, Chennai 600 008, Phone: 8262665 Fax: 8262331
e-mail: jpmedpub@md3.vsnl.net.in
• 1A Indian Mirror Street, Wellington Square
Kolkata 700 013, Phone: 2451926 Fax: 2456075
e-mail: jpbcal@cal.vsnl.net.in
• 106 Amit Industrial Estate, 61 Dr SS Rao Road, Near MGM Hospital
Parel, Mumbai 400 012 , Phones: 4124863, 4104532 Fax: 4160828
e-mail: jpmedpub@bom7.vsnl.net.in
VIVA—based on Vasudevan’s: Textbook of Biochemistry, 3rd Edition
© 2001, Jaypee Brothers Medical Publishers (P) Ltd

All rights reserved. No part of this publication should be reproduced, stored in a retrieval
system, or transmitted in any form or by any means: electronic, mechanical, photocopying,
recording, or otherwise, without the prior written permission of the editors and the publisher.
This book has been published on good faith that the material provided by editors is original.
Every effort is made to ensure accuracy of material, but the publisher, printer and editors
will not be held responsible for any inadvertent error(s). In case of any dispute, all legal
matters to be settled under Delhi jurisdiction only.
First Edition: 1995

Second Edition: 1998
Third Edition: 2001
Publishing Director: RK Yadav

Biochemistry Viva Questions

Transféré par

Informations du document

Copyright

Formats disponibles

Partager ce document

Partager ou intégrer le document

Options de partage

Avez-vous trouvé ce document utile ?

Ce contenu est-il inapproprié ?

Droits d'auteur :

Formats disponibles

Biochemistry Viva Questions

Transféré par

Droits d'auteur :

Formats disponibles

Cont

1. Cell Organells ....................................................... 1

2. Cell Membranes: Structure and Function ....... 3

3. Amino Acids: Structure and Properties ........... 8

4. Proteins: Structure and Function .................... 17

6. Enzymology-II: Iso-Enzymes and

7. Methods of Separation & Purification of

8. Carbohydrates-I:Chemistry, Digestion and

9. Carbohydrates-II: Major Metabolic

10. Carbohydrates-III: Regulation of Blood

11. Carbohydrates-IV: Other Metabolic Pathways

12. Lipids-I: Chemistry, Digestion and

13. Lipids-II: Metabolism of Fatty acids, Fatty acid

14. Lipids-III: Cholesterol, Lipoproteins and

15. Lipids-IV: MCFA, PUFA and

16. Lipids-V: Compound Lipids ......................... 118

17. Amino Acid Metabolism-I:

18. Amino Acid Metabolism-II: Simple,

19. Amino Acid Metabolism-III: Acidic, Basic and

20. Amino Acid Metabolism-IV: Aromatic Amino

21. Amino Acid Metabolism-V: Inter-relations of

22. Citric Acid Cycle .............................................. 144

23. Electron Transport Chain ............................... 147

24. Free Radicals and Anti-oxidants ................... 151

25. Plasma Proteins ................................................ 153

26. Immunochemistry ............................................ 156

27. Specialised Proteins: Collagen, Myosin ...... 158

28. Heme Synthesis and Breakdown ................. 160

29. Haemoglobins .................................................. 165

30. Vitamin-I: Fat Soluble Vitamins: A, D, E

31. Vitamin-II: Water soluble vitamins .............. 174

32. Mineral Metabolism ........................................ 189

33. Energy Metabolism and Nutrition ............... 195

34. Detoxification and Biotransformation of

35. Biochemical Aspects of Environmental

36. Acid Base Balance and pH ............................. 203

38. Molecular Biology-I: Nucleotides, Chemistry

39. Molecular Biology-II: DNA structure and

40. Molecular Biology-III: Transcription and

41. Molecular Biology-IV: Molecular Genetics

42. Molecular Biology-V: Recombinant DNA

43. Biochemistry of AIDS ..................................... 233

44. Biochemistry of Cancer ................................... 235

45. Applications of Radio-isotopes in

46. Body Fluids ....................................................... 240

47. Hormones-I: Mechanism of Action of

48. Hormones-II: Pituitary Hormones ................ 244

49. Hormones-III: Steroid Hormones ................. 246

50. Hormones-IV: Thyroid Hormones ............... 248

51. Clinical Biochemistry-I: .................................. 250

53. Clinical Biochemistry-III: Kidney Function

Q. What is the function of Golgi complex?

Q. What is the function of lysosomes?

Q. What are ecto-enzymes?

Q. What are the components of membrane that al-

Q. Give examples of active transport systems.

Q. How are co-transport systems classified?

Q. What is phagocytosis. (Page 11)

Q. How do you classify amino acids? (Page 12)

Q. What are the basic amino acids? (Page 12)

Q. Phenol group is present in which amino acid?

Q. Which amino acid is synthesised after it gets in-

Q. What is iso-electric point?. (Page 14)

Q. Can you name some substances where D-amino