Biochem Notes

1. Enzymes (concept). Common properties of enzymes and inorganic catalysts.
The specific properties of

enzymes.Chemical nature of enzymes, proofs?
Current theory: Induced fit model: As the substrate binds to the enzyme, the shape of the enzyme site changes
to accommodate the reaction.
Fisher lock and key model: enzyme lock, substrate key
Similarities and Differences between enzymes and catalysts

Similarities Differences
Both needed in little quantities Enzymes are complex proteins while catalysts are simple
inorganic molecules
Both accelerate the rate of reaction but can’t initiate Enzymes catalyze only biological reactions
one
Both decrease activation energy Enzymes are significantly affected by Temperature and
pH not so in catalysts
Both temporarily combine with substrate molecule Enzymes can be easily inactivated not so catalysts
Reaction accelerated by both is reversible Enzymes are regulated by specific substances called
cofactors but not in the case of catalysts
both do not alter nature and quantity of end product Enzymes catalyze a specific type of reaction while
catalysts have a wide range
Chemical Nature of Enzymes: All known enzymes are proteins. They are high molecular weight compounds made up
principally of chains of amino acids linked together by peptide bonds.
Many enzymes require the presence of other compounds - cofactors - before their catalytic activity can be exerted.
This entire active complex is referred to as the holoenzyme; i.e., apoenzyme (protein portion) plus the cofactor
(coenzyme, prosthetic group or metal-ion-activator) is called the holoenzyme.
Apoenzyme + Cofactor = Holoenzyme
Cofactor may be:

 A coenzyme – is a small, organic, non-protein molecules that carries chemical groups between enzymes e.g.
NAD+, CoA (carrier of acyl group)
 A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to
the protein or apoenzyme portion. Examples include flavin nucleotides and heme.
 A metal-ion-activator - these include K+, Fe++, Fe+++, Cu++ (cytochrome oxidase), Co++, Zn++, Mn++, Mg++,
Ca++, and Mo+++. E.g. zinc for carboxypepditase
2. The structure of simple and complex enzymes. Cofactors, a difference between coenzyme and prostetic
group. The role of apoenzyme and coenzyme in enzymatic reactions?
Prosthetic vs Coenzymes
Prosthetic Group Coenzyme
Prosthetic group is a type of a helper molecule which is a Coenzyme is a specific kind of cofactor molecule which is
non proteinaceous compound that helps enzymes to an organic molecule that helps enzymes to catalyze
perform their functions. chemical reactions.
Bond with Enzymes
They bind tightly or covalently with enzymes to aid They bind loosely with the active site of the enzyme to
enzymes. help catalytic function.
Composition
Prosthetic groups are metal ions, vitamins, lipids, or Coenzymes are vitamins, vitamin derivatives or
sugars. nucleotides.
Main Function
Prosthetic group mainly provides a structural Coenzyme mainly provides a functional
Removal from the Enzyme
Prosthetic groups – covalently bound to active site Coenzymes can be easily removed from the enzymes.
cannot be easily removed from the enzymes.
Examples
Examples include flavin nucleotides and heme. Examples include AMP, ATP, coenzyme A, FAD, and NAD+,
S-adenosyl methionine
Six classes of enzymes according to mechanism of action

Class Of enzymes Reaction carried out Example
Oxidoreductases Transfer of electrons – catalyze redox reaction Alcohol dehydrogenase
contains Zinc, Fe2+
typically found, NAD
Transferases Catalyze transfer of functional groups Hexokinase
Hydrolases Catalyze bond cleavage by hydrolysis i.e. with Trypsin, alkaline
water phosphatase, lysosomes
Lyases Catalyzed bond cleavage by elimination Pyruvate decarboxylase,
aldolase
Isomerases Catalyze a change in molecular structure i.e. Maleate isomerase
optical or geometric isomers
Ligases Catalyze the union of two molecules Pyruvate carboxylase,
located in ribosomes
Zymogens are activated by proteolytic activation
Enzymes:
Composed of proteins combined with non-protein structures (either organic or inorganic) that aid in their function:
 Coenzymes
 Cofactors – non protein part
 Prosthetic groups e.g. Iron porphyryn complex for cytochrome
Coenzymes: non protein portion of an enzymes

Apoenzyme: protein portion of an enzyme. Catalytically inactive by itself
Haloenzyme: complete catalytically active enzyme
Apoenzyme + Cofactor = Holoenzyme
Isozyme: enzymes with subtle molecular differences that catalyze the same reaction
An enzyme can be:

 Competitive: competes with substrate for active site
 Uncompetitive: binds to ES complex
 Allosteric
There are such three enzymes in pyruvate dehydrogenase complex: Pyruvate dehydrogenase, dihydrolipoyl acetyl
transferase, dihydrolipoyl dehydrogenase.
3. Characteristic of thermolability and specificity of enzyme action?

Specificity of Enzymes: Since the substrate must fit into the active site of the enzyme before catalysis can occur, only
properly designed molecules can serve as substrates for a specific enzyme
 Absolute specificity - the enzyme will catalyze only one reaction.
 Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino,
phosphate and methyl groups.
 Linkage specificity - the enzyme will act on a particular type of chemical bond regardless of the rest of the
molecular structure.
 Stereochemical specificity - the enzyme will act on a particular steric or optical isomer.

Specificity of enzyms is caused by all the following factors:
A. Conformational complementary
B. Electrostatic complementary
C. Structure of active site of enzyme
E. Proteins nature
4. The effect of pH on enzyme activity. Optimal pH for different enzymes?
Enzymes are affected by changes in pH. The most favorable pH value - the point where the enzyme is most active - is
known as the optimum pH.
Extremely high or low pH values generally result in complete loss of activity for most enzymes. pH is also a factor in
the stability of enzymes. As with activity, for each enzyme there is also a region of pH optimal stability
Enzymes pH Optimum Enzymes pH Optimum

Lipase (pancreas) 8.0 Urease 7.0
Lipase (stomach) 4.0-5.0 Amylase (pancreas) 6.7-7.0
Pepsin 1.5-1.6 Catalase – decompose 7.0
1.0-2.0 H2O2 require iron for
function
Trypsin 7.8-8.7 Salivary amylase (activated 6.6-6.8
by Cl-)
5. Active sites and allosteric site of enzymes?
Allosteric regulation:
 Allosteric enzyme: a regulatory enzyme that has both an active site (for the substrate) and an allosteric site
(for the effector)
 often catalyze the first step in a reaction pathway
 If the effector is present, it binds to the allosteric site causing a conformational change to the active site
which then changes (increase or decreases) the enzyme activity
 If no effector is present, the enzyme can still act on substrate (via the active site) to produce product
 A form of feedback regulation in which an enzyme of a metabolic pathway is controlled by the end product of
that same pathway
 Usually Participates in feedback regulation.
 Does not display Michaelis Menton kinetics
Types of Active Site: Because enzymes, like all proteins, are made of amino acids, they can create active sites with a
wide variety of properties that can bind specifically to different substrates. Properties of amino acids which enzymes
can use to bind to substrates include:
 Size and shape of active site – Can be created specifically to fit around a substrate.
 Polarity or non-polarity – Polar molecules are attracted to other polar molecules, while non-polar molecules
prefer other non-polar molecules. In this way, parts of the active site can attract or repel different parts of
the substrate to create a better fit.
 Positive or negative charge – When it comes to ions, opposites really do attract! Positive charges are
attracted to negative charges, and vice versa. Similar charges – two positive charges, for example – will
actively repel each other instead of attracting. This is another way in which an enzyme active site can attract
certain parts of substrates, while repelling others to create the right fit.
 Hydrophobicity or hydrophilicity – Just like with polarity, in this case “like attracts like.” Hydrophobic amino
acids attract other hydrophobic molecules, and hydrophilic amino acids attract hydrophilic substrates.
 Special properties of co-factors – Some vitamins and minerals are important because they are used as co-
factors that help enzymes bind to their substrates.
6. The origin of blood enzymes. Enzymes specific to different organs:

1. enzymes specific for heart; ASAT: aspartate amino transferase present in myocardiocytes, released if
myocardiocytes are damages i.e. during heart infarction another example is Lactate dehydrogenase
1, 2 its presence in blood may indicate heart disease, Creatin phosphokinase 2-4 hours after acute
heart pain
2. enzymes specific for liver; ALAT, alanine amino transferase present in hepatocytes, released to blood
up on hepatocyte damage i.e. Liver cirrhosis. another example is lactate dehydrogenase 4 and 5
Carbamoyl phosphate ornithine transferase in blood indicates inflammation of liver
3. enzymes specific for pancreas: pancreatic amylase is released to blood, indicate lyses of pancreatic
cells e.g. acute pancreatitis
7. The stages of metabolism in the organism. The scheme of specific and common pathways of proteins,
carbohydrates and lipids catabolism?
Central intermediate product of metabolism is: Acetyl-CoA
8. Biological functions of tricarboxylic acid cycle. NAD- and FAD- dependent reactions of Krebs cycle. Reaction of
substrate-level phosphorylation?
Functions of Citric acid cycle:

 Primary function is to provide energy ATP
 It is the final common pathway for the oxidation of carbohydrates, lipids and proteins via acetyl CoA or
intermediates of the cycle
 Citric acid cycle is an amphibolic process i.e. it plays a role in both oxidative (catabolic) and synthetic
(anabolic) process e.g. Gluconeogenensis, transamination, fatty acid synthesis and porphyrin synthesis
 Oxidation of acetic acid into СО2 and Н2О
 Donator of hydrogen atoms for respiratory chain
 Formation of ATP
 Supplying substrates for heme synthesis
Citric acids Cycle overall reaction:
Citric acids Cycle:

 Occurs in the mitochondrial matrix
 Tightly regulated by both ATP and NAD+
 Completes the metabolism of glucose
 Carrier is oxaloacetate
 Isocitrate dehydrogenase is an allosteric enzyme that controls the rate of TCA
Substrate-level phosphorylation occurs in the cytoplasm of cells during glycolysis and in mitochondria during the
Krebs cycle (succinate thiokinase) under both aerobic and anaerobic conditions. In the pay-off phase of glycolysis, a
net of 2 ATP are produced by substrate-level phosphorylation.
Substrate level phosphorylation is the synthesis of ATP by direct transfer of phosphate group from a substrate (high
energy intermediate) to a molecule of ADP (occurs in glycolysis and the TCA cycle)
Oxidative Phosphorylation the use of oxygen to oxidise electron carriers NADHin order to generate ATP. ATP is made
via a mechanical reaction. Occurs during the electron transport chain
Process Location Phosphorylation Net ATP per Glucose

Embden Meyerhof pathway Cytosol Substrate level 2
(glycolysis)
Entner doudoroff pathway Cytosol Substrate level 1
(bacterial metabolism)
TCA cycle Mitochondrial matrix Substrate level 2 as GTP in succinate
dehydrogenase step (24 in
total- 12 per acetyl CoA) or 1
ATP per turn
ETC Inner mitochondrial membrane Oxidaive 32 (G3P shuttle)
34 (malate-aspartate shuttle)
9. What is macroergic bond? Examples of high energy compounds?
Macroergic bond is a high energy bond present in some phosphorus containing compounds in living organisms e.g.
Adenosine triphosphate and ADP. Compounds that contain these bonds are known as phophagen.
High-energy phosphate bonds are pyrophosphate bonds, acid anhydride linkages formed by taking phosphoric acid
derivatives and dehydrating them. As a consequence, the hydrolysis of these bonds is exergonic under physiological
conditions, releasing energy.
Energy released by high energy phosphate reactions Reaction ΔG [kJ/mol]

ATP + H2O → ADP + Pi -30.5
ADP + H2O → AMP + Pi -30.5
ATP + H2O → AMP + PPi -40.6
PPi + H2O → 2 Pi -31.8
AMP + H2O → A + Pi -12.6
These reactions are, in general, not allowed to go uncontrolled in the human cell but are instead coupled to other
processes needing energy to drive them to completion. Thus, high-energy phosphate reactions can:
 provide energy to cellular processes, allowing them to run
 couple processes to a particular nucleoside, allowing for regulatory control of the process
 drive a reaction out of equilibrium (drive it to the right) by promoting one direction of the reaction faster
than the equilibrium can relax.
ATP and energy coupling
Cells make endergonic reactions happen by supplying them with free energy released by exergonic reactions. Energy
coupling is the transfer of energy from one reaction to another in order to drive the second reaction
Example
10. Ways of ATP formation in the organism. What is tissue respiration? Structure and functions of respiratory
chain?
Tissue respiration: is the process by which food substances are broken down in living cells. A large amount of energy
is released for the cells to perform different activities. In tissue respiration, glucose combines with oxygen to release
energy, carbon dioxide and water
Overall: Glucose + Oxygen → CO2 + H2O + Energy
Ways of ATP formation:
 Substrate-level phosphorylation occurs in the cytoplasm of cells during glycolysis and in mitochondria during
the Krebs cycle under both aerobic and anaerobic conditions. In the pay-off phase of glycolysis, a net of 2 ATP
are produced by substrate-level phosphorylation. Substrate level phosphorylation is the synthesis of ATP by
direct transfer of phosphate group from a substrate (high energy intermediate) to a molecule of ADP (occurs
in glycolysis and the TCA cycle)
 Oxidative Phosphorylation the use of oxygen to oxidise electron carriers NADHin order to generate ATP. ATP
is made via a mechanical reaction. Occurs during the electron transport chain
Process Location Phosphorylation Net ATP per Glucose

Embden Meyerhof pathway Cytosol Substrate level 2
(glycolysis)
Entner doudoroff pathway Cytosol Substrate level 1
(bacterial metabolism)
TCA cycle Mitochondrial matrix Substrate level 2 as GTP
ETC Inner mitochondrial membrane Oxidaive 32 (G3P shuttle)
34 (malate-aspartate shuttle)
ATP production per Molecule of glucose

Metabolic Pathway ATP produced
Glycolysis (cytosol)
 2 ATP consumed (by hexokinase and PFK) -2
 4 ATP formed +4
 2 NADH formed
Pyruvate → Acetyl CoA (mitochondrial matrix)
 2 NADH formed
TCA Cycle (mitochondrial matrix)
 2 GTP formed +2
 6 NADH formed
 2 FADH2 formed
ETC (inner mitochondrial membrane)
 10 NADH oxidized +30
 2 FADH2 oxidized +4
+38
Note: NADH yields 3 ATP and FADH2 yields 2 ATP
11. Classification and representatives of carbohydrates. Biological functions of carbohydrates in the organism?
Classification of carbohydrates:
Chemical Classification Physiological Classification
Monosaccharides: the simplest carbohydrates further Simple or Complex
classified:  Simple: mono- and disaccharides (also known as
 # of carbon atoms: Trioses, tetroses, pentose, “sugars”) and tri- and tetrasaccharides
hexoses, heptoses (oligosaccharides)
 Functional Groups: Aldoses (aldehyde) or  Complex: the polysaccharides
ketoses (ketone). Reducing sugars contains
aldehyde groups that are oxidised to
carboxylic acids e.g. glucose, fructose, lactose
 Isomerism: D-Form (most common or L-form
Disaccharides: Glycosidic condensation of two Classified according to energy purposes i.e. available or not
monosaccharides available
 Maltose: 2 glucose via maltase  Available: as glucose, fructose, galactose between
 Sucrose: glucose + fructose via sucrose monosaccharides, sucrose, lactose, maltose and
 Lactose: glucose + galactose via lactase maltodextrin between oligosaccharides, and starch
Oligosaccharides: Glycosidic condensation of 2-10 and glycogen between polysaccharides;
monosaccharides  Not Available: as xylose (monosaccharide),
Polysaccharides: Glycosidic condensation of >10 lactulose (see lactose) and raffinose (respectively di-
monosaccharides and trisaccharide), fiber (cellulose, hemicellulose,
 Mostly used as storage molecules or cellular lignin, pectins etc.) and resistant or not digestible
structural component starch (polysaccharides
 Can be linear or branched
Functions of polysaccharides:
1. Storage of polysaccharides:
 Starch: A homopolymer of glucose linked by α-1, 4 glycosidic bonds. Contains unbranched helical amylose
and branched amylopectin
 Glycogen: a homopolymer of glucose linked by α-1, 4 glycosidic bonds. Contains numerous branch points via
α-1, 6 glycosidic linkages
2. Structural polysaccharides:
 Glycosaminoglycan’s (GAGs): heteropolymer chains containing repeating disaccharide units of an amino
sugar and an uronic acid. Major structural polysaccharides of extracellular matrix (ECM). Connective tissue
(CT) and outer cell membrane surfaces.
 Proteoglycans: complex carbohydrates that have a central protein molecule to which many GAGs are
attached. 95% polysaccharides and 5% proteins. Located in ECM
 Cellulose: major component of plants
3. Provide instant energy to the body: This appears to be the primary function of carbohydrates in the body.
4. Reserve food for the body emergency: The excess glucose in the body is converted to glycogen due to the
stimulation by the hormone insulin.
5. Carbohyrdrates form other bio molecules: Carbohydrates in excess are converted into other bio-molecules
of physiological importance like fats, by fatty acid synthesis reaction in the cell for storage in the body and
use in times of starvation.
6. Constitute genetic material: Carbohydrates form a part of genetic material like DNA and RNA in the form of
deoxyribose and ribose sugars. This as carbohydrates form heptulose sugars which are used to form ribose
sugars (pseudo-heptulose pathway)
7. Detoxification of the body by metabolism: Many drugs, toxic wastes in the body are metabolized for easy
excretion in the body. Some of these are water insoluble and hence they are difficult to be expelled in urine.
Body converts them into glucouronyl conjugates using the glucouronyl moiety derived from carbohydrates.
A carbohydrate moiety like glucose combines with uronic acid to form glucouronate. These conjugates of
insoluble substances with glucouronyls are more water-soluble and easily excreted from the body. Thus
detoxification of physiological importance is carried out to some extent with carbohydrate derivatives
12. Digestion of carbohydrates: localization, types, role of enzymes?

13. Energetic balance of glycolysis in aerobic conditions. Energetic balance of glycolysis in anaerobic conditions.
Biological role of glycolysis?
Aerobic Respiration
 If oxygen is present, the pyruvate is transported to the mitochondria for further breakdown (complete
oxidation)
 This further oxidation generates large numbers of reduced hydrogen carriers (NADH + H+ and FADH2)
 In the presence of oxygen, the reduced hydrogen carriers can release their stored energy to synthesise more
ATP
 Aerobic respiration involves three additional processes – the link reaction, krebs cycle and the electron
transport chain
Anaerobic Respiration (Fermentation)
 If oxygen is not present, pyruvate is not broken down further and no more ATP is produced (incomplete
oxidation)
 The pyruvate remains in the cytosol and is converted into lactic acid (animals) or ethanol and CO2 (plants and
yeast)
 This conversion is reversible and is necessary to ensure that glycolysis can continue to produce small
quantities of ATP
o Glycolysis involves oxidation reactions that cause hydrogen carriers (NAD+) to be reduced (becomes
NADH + H+)
o Typically, the reduced hydrogen carriers are oxidised via aerobic respiration to restore available
stocks of NAD+
o In the absence of oxygen, glycolysis will quickly deplete available stocks of NAD+, preventing further
glycolysis
o Fermentation of pyruvate involves a reduction reaction that oxidises NADH (releasing NAD+ to
restore available stocks)
o Hence, anaerobic respiration allows small amounts of ATP to be produced (via glycolysis) in the
absence of oxygen
14. Diabetes mellitus: types, causes, disorders of metabolism, symptoms, treatment?

Diabetes mellitus is a chronic disease involving the in ability of cells in the body from uptake glucose due to lack of
insulin, inability of body to use insulin or both.
There are three major types of diabetes:
1. Type 1 diabetes: (insulin dependent diabetes), It's caused by the body attacking its own pancreas with
antibodies. In people with type 1 diabetes, the damaged pancreas doesn't make insulin. This type of diabetes
may be caused by a genetic predisposition. It could also be the result of faulty beta cells in the pancreas that
normally produce insulin. Treatments: Insulin pens, Syringe
2. type 2 diabetes: (non-insulin dependent diabetes), With Type 2 diabetes, the pancreas usually produces
some insulin. But either the amount produced is not enough for the body's needs, or the body's cells are
resistant to it. Insulin resistance, or lack of sensitivity to insulin, happens primarily in fat, liver, and muscle
cells Controlled: weight management, nutrition, medication
3. gestational diabetes: Diabetes that's triggered by pregnancy is called gestational diabetes (pregnancy, to
some degree, leads to insulin resistance)
Diabetic tendency can be detected by the glucose-tolerance test.

Test by sugar loading 1 g per 1 kg of weight
Symptoms: hyperglycemia, hyperketonemia. In the urine are glucose, ketone bodies accumulate in blood
Steroid diabetes: high level of 17-ketosteroids in urine

15. Biological role and classification of lipids. Fatty acids: structure, role. Essential fatty acids?
PHYSIOLOGICAL ROLE OF LIPIDS
 Energetic role (fuel molecules)
 Components of membranes (structural role)
 Precursors for many hormones (steroids)
 Signal molecules (prostaglandins)
 Protective role (lipids surround important organs)
 Enzyme cofactors (vitamin K)
 Electron carriers (ubiquinone)
 Insulation against temperature extremes
Lipid Function
Cholesterol Structural component of membranes; precursor for bile acid and steroid synthesis
Fatty acids Energy source
Triglycerides Energy store
Phospholipids Structural components of membranes
Eicosanoids Multiple, including effect on blood coagulation, bronchial and vascular contractility,
reproduction
Sphingolipids CNS, Blood group substance
Classification of lipids
Essential Fatty acids:
 Linolenic acid: Omega 3 fatty acid
 Linoleic acids: Omega 6 fatty acid
 Oleic acids: Omega 9 fatty acid
 Arachidonic acids
16. Biological role of cholesterol. Contents of cholesterol in blood, transport forms?

Biological role of cholesterol
 Cholesterol is an essential lipid constituent of cell membranes
 Cholesterol is a precursor of steroid hormones and of bile acids
 Intermediates of cholesterol biosynthesis are required to make vitamin D and for posttranslational
modification of membrane proteins
 Cholesterol transported to liver as High density lipoproteins
Cholesterol chart for adults
Total cholesterol HDL cholesterol LDL cholesterol Triglycerides
Good Less than 200 40 or higher Less than 100 Less than 149
Borderline 200–239 n/a 130–159 150–199
High 240 or higher n/a 160 or higher 200 or higher
Low n/a less than 40 n/a n/a
Synthesis of Cholesterol
Three stages of cholesterol biosynthesis
1. Synthesis of isopentenyl pyrophosphate, that is the key building block of cholesterol, from acetyl CoA
2. Condensation of six molecules of isopentenyl pyrophosphate to form squalene
3. Squalene cyclizes and the tetracyclic product is converted into cholesterol
Transport of cholesterol in blood
Cholesterol travels in the blood transported in molecules called lipoproteins. These are sphere shaped assemblies
(containing lipids and proteins) that keep the cholesterol separated from the blood due to the soluble nature of the
assemblies.
LDL is the major carrier of cholesterol in the blood taking it to peripheral tissues. It is taken up by cell mediated
endocytosis. Cells of all organs have LDL receptors. Receptors for LDL are localized in specialized regions called coated
pits, which contain a specialized protein called clathrin Apo B-100 on the surface of an LDL binds to the receptor
Receptor-LDL complex enters the cell by endocytosis. Endocytic vesicle is formed. Vesicle fuse with lysosomes
Lysosomal lipases and proteases degrade LDL LDL receptor itself returns to the plasma membrane Apo B-100 is
hydrolyzed to amino acids Cholesteryl esters are hydrolyzed to free cholesterol and fatty acids
Released free cholesterol:

 is incorporated into the membranes or
 is reesterified for storage inside the cell by the enzyme acyl CoA:cholesterol acyltransferase (ACAT)
Feedback regulation:
Abundance of intracellular cholesterol suppresses the synthesis of LDL receptors and so the uptake of additional
cholesterol from plasma LDL is blocked
Lipid Transport
Lipoproteins
 Transport lipids in blood plasma
 Composed of a non-polar core surrounded by a single layer of amphipathic phospholipids and cholesterol
 Characterized by the protein moiety embedded in their outer layer (apoprotein)
 Contain triglycerides 156%, phospholipids (30%) cholesterol (14%) cholesterol esters (36%) and free fatty
acids 4%
Filmilial Hypercholesterolemia is caused by an autosomal dominant defect of the low density lipoprotein (LDL)
receptor, leading to increased plasma LDL cholesterol and atherosclerosis
The desirable level of cholesterol in blood plasma: < 200 mg/dl (< 5 mmol/l)
For a healthy person, the LDL/HDL ratio is 3.5
17. Pathologies of lipids metabolism?
18. Biological role of proteins in the organism. Nitrogenous balance. Protein standards in nutrition. Essential and
nonessential amino acids?
Biological role of proteins

Type Examples Occurrence/ Function
Contractile Proteins Actin Thin Filament
Myosin Thick filament
Dynein Cilia and flagella
Enzymes/ Catalysts Hexokinase Phosphorylates glucose
Lactate Dehydrogenase forms lactate Dehydrogenates lactate
under anaerobic condition
Cytochrome C Transfer electrons
DNA polymerase Replicates and repairs DNA
Hormones/ Regulatory Insulin Regulate glucose metabolism
ACTH Regulate corticosteroid synthesis
Growth Hormone Stimulate bone growth
All receptors are proteins
Structural Collagen
Transport Hemoglobin O2 and CO2 Transport in blood
Albumin Transport free fatty acids in blood
Transferrin Transport Iron in blood
Myoglobin Carries O2 in muscles
Defense Clotting factor Prevent blood loss
Immunoglobulins Protect against infection
Storage Seeds and eggs
Ferritin Stores iron In the spleen and liver
19. Transamination and decarboxilation of amino acids, mechanism, role of enzymes and coenzymes?
The general ways of amino acids degradation:

 Deamination
 Transamination
 Decarboxylation
The major site of amino acid degradation: the liver
Deamination of amino acids

Deamination: elimination of amino group from amino acid with ammonia formation.
Four types of deamination:
 oxidative (the most important for higher animals):
 reduction: R-CH(NH2)-COOH (amino acid) + 2H→R-CH2-COOH (fatty acid) + NH3
 hydrolytic: R-CH(NH2)-COOH (amino acid) + H2O → R-CH(OH)-COOH (hydroxyacid) + NH3 (ammonia)
 intramolecular: R-CH(NH2)-COOH (amino acid) → R-CH-CH-COOH (unsaturated fatty acids) + NH3
Oxidative deamination
L-Glutamate dehydrogenase plays a central role in amino acid deamination
In most organisms glutamate is the only amino acid that has active dehydrogenase
Transamination: transfer of an amino group from an alpha amino acid to an alpha keto acid (usually to
Alpha ketoglutarate)
Enzymes: aminotransferases (transaminases).
There are different transaminases, T h e most common:

 alanine aminotransferase (transports ammonia to liver): alanine + α ketoglutarate ↔ pyruvate + glutamate
 aspartate aminotransferase: aspartate + α-ketoglutarate ↔ oxaloacetate + glutamate
Aminotransferases funnel α-amino groups from a variety of amino acids to α-ketoglutarate with glutamate formation
Glutamate can be deaminated with NH4 + release
Mechanism of transamination
All aminotransferases require the prosthetic group pyridoxal phosphate (PLP), which is derived from pyridoxine
(vitamin B6).
Ping-pong kinetic mechanism
 First step: the amino group of amino acid is transferred to pyridoxal phosphate, forming pyridoxamine
phosphate and releasing ketoacid.
 Second step: α-ketoglutarate reacts with pyridoxamine phosphate forming glutamate
Decarboxylation of amino acids
Decarboxylation: removal of carbon dioxide from amino acid with formation of amines. Usually amines have high
physiological activity (hormones, neurotransmitters etc).
Enzyme: decarboxylases
Coenzyme: pyrydoxalphosphate
Significance of amino acid decarboxylation

1. Formation of physiologically active compounds: e.g. Glutamate is decarboxylated to GABA, histidine is
decarboxylated to histamine
2. Catabolism of amino acids during the decay of proteins: Enzymes of microorganisms (in colon; dead organisms)
decarboxylate amino acids with the formation of diamines.
20. Hormones as biological regulators. Hormonoids (histohormones). Endocrine glands. Classification of

hormones?
Hormones: organic biologically active compounds of different chemical nature that are produced by the endocrine
glands, enter directly into blood and accomplish humoral regulation of the metabolism of compounds and functions
on the organism level. Hormones provide a long term sustained response unlike Nervouse regulatory system which
provide a short term response
Hormonoids (tissue hormones): compounds that are produced not in glands but in different tissues and regulate
metabolic processes on the local level (e.g. Kinins), but some of them (serotonin, acetylcholine) enters blood and
regulate processes on the organism level.
Specific stimulus for hormones secretion is:

 nervous impulse
 concentration of the certain compound in blood passing through the endocrine gland
Classification of hormones according to chemical nature:

1. Proteins: hormones of anterior pituitary (except ACTH), insulin, parathyroid hormone.
2. Peptides: ACTH, calcitonin, glucagon, vasopressin, oxytocin, hormones of hypothalamus (releasing factors
and statins).
3. Derivatives of amino acids: catecholamine (epinephrine and norepinephrine), thyroxin, triiodothyronine,
hormones of epiphysis. And insulin
4. Steroid (derivatives of cholesterol): hormones of the cortex of epinephrine glands, sex hormones.
5. Derivatives of polyunsaturated fatty (arachidonic) acids: prostaglandins (20 carbon atoms)
The Final effect of hormones

1. Change the permeability of cell membrane, accelerate the penetration of substrates, enzymes, coenzymes
into the cell and out of cell.
2. Acting on the allosteric centers affect the activity of enzymes (Hormones penetrating membranes).
3. Affect the activity of enzymes through the Secondary messengers (cAMP). (Hormones that cannot penetrate
the membrane).
4. Act on the genetic apparatus of the cell (nucleus, DNA) and promote the synthesis of enzymes (Steroid and
thyroid hormones).
Inactivation of hormones
After biochemical effect hormones are released and metabolized. Hormones are inactivated mainly in liver
Inactive metabolites are excreted mainly with urine
Half-time life
 from several min to 20 min – for the majority of hormones
 till 1 h – for steroid hormones
 till 1 week – for thyroid hormones
21. Hormones of anterior pituitary (7 hormones). Why these hormones are called “tropic” hormones?
Hormone Released Chemical Class Target tissues/ organs Chief function of hormones
Thyroid Stimulating Glycoprotein Thyroid Stimulates thyroid to release T3 and T4
hormone TSH
Adrenocorticotropic ACTH Peptide Adrenal cortex Stimulates adrenal cortex -Secretion of
(Cushing disease hyper glucocorticoid, mineralocorticoid and
secretion of ACTH) androgens
Follicle stimulating Glycoproteins Gonads Sex hormone production
hormone
Prolactin PRL Protein Mammary gland Milk production
Growth hormone GH Simple Protein Soft tissue, bones Cell division, protein synthesis and bone
(hyper secretion leads to growth
gigantism)
Melanocyte stimulating Peptide Melanocytes in skin Regulate skin color
hormone MSH
Luteinizing Hormone Glycoprotein Gonads Sex hormone production
They are called tropic hormones as they stimulates somatic growth of organs and tissues, particularly bones,
cartilages, muscles
22. Somatotropic hormone: structure, effect on protein, carbohydrate and lipid metabolism. Clinical
manifestations of the changing of somatotropic hormone concentration in children and adults?
Chemical nature: simple protein

It is secreted continuously during the whole life
Secretion is stimulated by somatoliberin, is inhibited by somatostatin
Main function: stimulates somatic growth of organs and tissues, particularly bones, cartilages, muscles
Carbohydrate Protein Lipid

Anti-insulin hormone – activates Promotes the entrance of AA into Stimulates the decomposition of
insulinase of liver cells lipids (lipolysis)
Activates the exit of glucose from Activates the synthesis of proteins, Stimulates the oxidation of fatty acids
liver DNA, RNA.
Inhibits the conversion of glucose Inhibits catabolism of proteins and
into fat AA
In the inherited hypoplasia of pituitary gland dwarfism is developed. For the treatment GH is used.
Hyper production of GH before puberty and before the completion of ossification results in gigantism
Hyper function of pituitary in adults results in acromegaly: un-proportionally intensive growth of particular body
parts (fingers, nose, lower jaw, tongue, inner organs). Cause: tumor of anterior pituitary
23. Thyrotropic, adrenocorticotropic and follicle stimulating hormone: chemical structure, biological role?
Adrenocorticotropic hormone (АCTH)

Chemical nature: polypeptide
Secretion is stimulated by corticoliberin
Feedback regulation of the speed of secretion depending on the cortisol level
Controls the cortex of epinephrine gland where cortisol is produced:

 promotes the increase of cholesterol content in epinephrine glands cortex and its conversion into
corticosteroids;
 activates the passing of glucose into epinephrine glands and pentose phosphate cycle (NADPH2 and pentose
synthesis)
 has melanocyte stimulating activity
 activates Gluconeogenesis
 Decreases glycolysis
Thyrotrophic hormone (ТТH)

Chemical structure: protein (glycoprotein)
Secretion is stimulated by thyroliberin
The speed of secretion is regulated according to the feedback regulation by thyroid hormones
It is necessary for the normal functioning of thyroid gland:

 promotes the accumulation of iodine in thyroid gland and its insertion into tyrosine;
 stimulates the synthesis of try- and tetraiodthyronin
Gonadotropic hormones
Follicle-stimulating
Chemical nature: protein (glycoprotein)
Secretion is stimulated by foliliberin
Function: stimulates the function of follicles in women and spermatogenesis in men
Luteinizing hormone
Chemical nature: protein (glycoprotein)
Secretion is stimulated by luliberin
Function: stimulates the follicular growth and conversion of the follicle into a corpus luteum in women and secretion
of testosterone in men
24. Hormones of posterior pituitary (3 hormones)?
Hormone Released Chemical Class Target tissues/ organs Chief function of

hormones
Antidiuretic hormone/ peptide Kidneys Stimulates water
Vassopressin reabsorption by kidneys
Oxytocin Peptide Uterus, Mammary gland Stimulates uterine muscle
contraction, release of milk
by mammary gland
25. Iodine containing hormones of thyroid gland. Effect of these hormones on protein, carbohydrate, lipid
metabolism?
Hormone Released Chemical Class Target tissues/ organs Chief function of hormones
Thyroxine T4 and Iodinated amino All tissues Increases metabolic rate, regulates
triiodothyronine T3 acids – derivatives of growth and development
– hypersecretion amino acids
results in Goiter,
Hypo secretion –
cretinism/
myoxedema (in
adults)
Calcitonin Peptide Bones, kidneys, intestines Raises blood calcium and phosphate
(Hypersecretion level
Hypocalciemia,
hypophosphatemia,
hyperphosphaturia)
Effect of T4 and T3 on Metabolism

Accelerate the absorption of In physiological concentration Activate the exit of lipids from depot,
carbohydrates in the intestine stimulate synthesis of proteins, its decomposition and oxidation
nucleic acids
Activate the decomposition of In the increased concentration
glycogen activate the protein decomposition
26. Hormones of pancreas (4 hormones)?
Hormone Cells involved Chemical Target tissues/ organs Chief function of hormones
Released Class
Insulin Beta cells of Protein Liver, muscle, adipose Lowers blood glucose level, by
Langerhans tissue, myocytes and glucose phosphorylation oppression
adipocytes
promotes formation of glycogen
Activates oxidization of glucose in
glycolysis, activates a PPP, activates
glycogen synthase (synthesis of
glycogen)
Activates synthesis of fats, represses
a gluconeogenesis
Insulin Activates a transport of

potassium into a cells, and sodium
from the cells
Glucagon Alpha cells of Peptide Liver, muscle, adipose increases blood glucose level,
Langerhans tissue promotes break down of glycogen -
glycogenolysis
Somatostatin Delta cells of Peptide Inhibits secretion of insulin and
Langerhans glucagon
Lipocain Epithelium of Activates the synthesis
ducts- of phospholipids in liver
pancreatic duct
27. Insulin: chemical structure, proinsulin, regulation of insulin production, target tissue for insulin. Effect of
insulin on carbohydrate, lipid, protein metabolism?
 Nature: protein (51 АA)

 Is formed from protein proinsulin by partial proteolysis
 Contains zinc
 Regulation of the synthesis:

o Glucose concentration in blood
o Other hormones (somatostatin)
o Sympathetic and parasympathetic nervous system
It is destroyed by insulinase (enzyme of liver) to amino acids

Target cells:
 Hepatocytes
 Myocytes
 Adipocytes
In the insufficiency: diabetes mellitus
Effect of Insulin
Activates glucokinase (hexokinase) Increases the permeability of Activates of the lipids synthesis
phоsphоfructokinase, pyruvatkinase membranes for AA Activates the synthesis of fatty acids
in glycolysis
Activates TAC (citrate synthase Activates synthesis of proteins and Promotes the saving of fats activating
nucleic acids the decomposition of carbohydrates
Activates PPC (G-6-PDH) Inhibits gluconeogenesis Inhibits gluconeogenesis
Activates glycogen synthase It depresses mobilization of fat from
a depot
Activates pyruvate- and alpha-
ketoglutarate dehydrogenase
Inhibits gluconeogenesis
Inhibits the decomposition of
glycogen (glucose-6-phosphatase)
Activates transfer of glucose through
the cells membranes
28. Sex hormones: kinds, structure, place of synthesis?
Sex hormones released by Gonads
Endocrine Hormone Released Chemical Target tissues/ organs Chief function of hormones
Gland Class
Testes Androgens – Steroid Gonads, skin, muscle and Stimulates male sex characteristics
Testosterone bones
Ovaries Estrogen and Steroid Gonads, skin, muscle and Stimulates female sex characteristics
progesterone bones
Estrogens
Nature: steroids
 Estradiol – is formed in follicles of ovarium
 Estron and estriol – are formed in liver and placenta in the metabolism of estradiol
Functions of estrogens
 Development of the female reproductive system organs
 Ability to fertility in reproductive period
Biochemical functions of estrogens
 Anabolic action on the tissues of reproductive organs
 Inhibit the exit of Ca from bones (osteoporosis in menopause)
Progesterone
Nature: steroid
Is formed in corpus luteum, placenta and epinephrine glands
Functions of progesterone
 Prepares the endometrium of uterus to implantation of ovum
 Inhibits the uterus contraction during pregnancy
 Stimulates the growth of mammary glands
Androgens
Testosterone
Nature: steroid
Is formed in the interstitial cells of testis, Is excreted as 17-кetosteroids
Functions of testosterone
 Development of the primary sex features
 Development of the secondary sex features
 Stimulates spermatogenesis
Biochemical functions of testosterone
 Strong anabolic action (stimulates the synthesis of NA, proteins, phospholipids), increases the mass of
muscles
 Keeps the Ca and P in organism
29. Hormones of adrenalcortex - corticosteroids. Two groups of corticosteroids?

Adrenal Gland
Endocrine Hormone Released Chemical Target tissues/ organs Chief function of hormones
Gland Class
Adrenal Glucocorticoids Steroid All tissues Raise blood glucose level, stimulate
Cortex (cortisol) break down of proteins, amino acids
in blood- gluconeogenesis
Mineralocorticoids Steroid Kidneys Reabsorb sodium and excrete
(aldosterone) potassium
Sex hormones Steroid Gonads, skin, muscles, Stimulate reproductive organs and
bones bring about sex characteristics
Adrenal Epinephrine and Modified Cardiac and other muscles Released in emergency situations,
Medulla norepinephrine amino acid raises blood glucose level through
Catecholamine proteins glycogenolysis through
glycogenphosphorylase
Catabolized by
Monoaminooxidase Activates a tissue lipase and
mobilization of fat from a depot
Promote protein catabolism
Increase lipolysis in fatty tissue
Hormones of Adrenal cortex:

Corticosteroids: There are more than 50 corticosteroids
Nature: steroids
Synthesized from cholesterol
Two groups:
 glucocorticoids (protein, carbohydrate and lipid metabolism)
 mineralocorticoids (mineral metabolism)
Glucocorticoids
Most important: corticosteron, cortison, hydrocortison
Synthesis is regulated by ACTH
Are transported combined with proteins
Half-life time: up to 1 hour
In the decomposition17-ketosteroids are formed (excretion with urine). Diagnostic significance – index of the
function of cortex of epinephrine glands and testis
Functions
 Anti-inflammatory, ant allergic, autoimmune
 Adaptive effect
 Maintain the blood pressure
 Maintain the volume of extracellular liquid
Increase the glucose level: Stimulate catabolic processes in Activate lipolysis
• Activate gluconeogenesis connective, lymphoid and muscle
• Inhibit hexokinase (glycolysis) tissues
Activate protein synthesis in liver Activate the conversion of FA into
carbs
Stimulate amino transferases
Stimulate the urine biosynthesis
30. Concepts "vitamin" and "provitamin".Classification of vitamins. Chemical and physiological name,
coenzymes, biological role of vitamins B1. Manifestations of hypovitaminosis, nature sources and day
requirement of vitamins B1?
Vitamin B1 – thymine antineurotic, consists of 2 rings a pyrimidine and a thiazole. Vitamin B1 is phosphorylated in
the liver to TMP, TPP – thiamine pyro phosphate (involved in oxidative decarboxylation), Thiamine diphosphate and
TTP who are coenzymes of pyruvate and alpha ketoglutarate dehydrogenase and transketolase.
In the thiamin deficiency:

 ketoacids that are toxic for nervous system are accumulated.
 Acidosis.
 Carbs are not used, energy deficit.
 Organism uses lipids and proteins, loss of
 weight, dystrophy, growth retardation.
 Catabolism prevails.
 Inhibition of transketolase, inhibition of
 PPC, deficit of NADPH and riboses,
 disorders of fatty acids synthesis, steroid
 hormones, cholesterol, nucleic acids
 Inhibition of transketolase, inhibition of PPC, deficit of NADPH and riboses, disorders of fatty acids synthesis,
steroid hormones, cholesterol, nucleic acids
 loss of weight, general weakness, pain in the area of heart, petehial hemorrhages, bleeding of gums, loss of
teeth
Chronic deficiency of Thiamine can lead to: Beri Beri disease (inactivity of pyruvate dehydrogenase, people who
consume polished rice are prone to beri beri) and Wernicke-Korsakoff syndrome
Natural sources: fish, lean meat and milk and fortified bread and cereals
Daily requirements: 1-3mg
Vitamin B1 is used for preparation of cocarboxylase

Vitamins: low molecular weight organic compounds that have different chemical structure and are not synthesized or
are synthesized in small amount in the human organism, are not used as building material, but have marked
biological effect and are necessary components of diet. They are classified as water and fat soluble
Pro-vitamin is a substance that may be converted within the body to a vitamin. E.g. "Provitamin B5" is a name for
panthenol, which may be converted in the body to vitamin B5 (pantothenic acid), pro-vitamin A" is a name for β-
carotene which has only about 1/6 the biological activity of retinol (vitamin A); the body uses an enzyme to convert
β-carotene to retinol
31. Concepts "avitaminosis", "hypervitaminosis" and "hypovitaminosis".Chemical and physiological name,

coenzymes, biological role of vitamins B2. Manifestations of hypovitaminosis, nature sources and day
requirement of vitamins B2?
Hypovitaminosis: decrease of vitamin amount in the organism

Hypervitaminosis: increase of vitamin amount in the organism
Avitaminosis: lack of vitamin in the organism
Cofactors are molecules that attach to an enzyme during chemical reactions. In general, all compounds that help
enzymes are called cofactors. However, cofactors can be broken down into three subgroups based on chemical
makeup and function:
Coenzymes: These are reusable non-protein molecules that contain carbon (organic). They bind loosely to an enzyme
at the active site to help catalyze reactions. Most are vitamins, vitamin derivatives, or form from nucleotides. They
typically are produced from vitamins such as B vitamins. examples of coenzymes are NAD (derived from Vitamin B 3)
and Coenzyme A (derived from Vitamin B5), FMN and FAD
Cofactors: Unlike coenzymes, true cofactors are reusable non-protein molecules that do not contain carbon
(inorganic). Usually, cofactors are metal ions such as iron, zinc, cobalt, and copper that loosely bind to an enzyme’s
active site. They must also be supplemented in the diet as most organisms do not naturally synthesize metal ions.
Prosthetic groups: These can be organic vitamins, sugars, lipids, or inorganic metal ions. However, unlike coenzymes
or cofactors, these groups bind very tightly or covalently to an enzyme to aid in catalyzing reactions. These groups are
often used in cellular respiration and photosynthesis.
Vitamin В2 (riboflavin, growth vitamin) Is composed from:

 isoallaxasine and
 alcohol ribitol
Functions of vitamin B2:
 Forms the coenzymes FMN and FAD which are necessary for the action of more than 30 enzymes – oxido-
reductases (оxidation-reduction reactions)
 AA deamination (оxidases of AA)
 pyruvate dehydrogenase and alphaketoglutarate complexes
 succinate dehydrogenase to fumarate (Krebs cycle)
 Fatty acids oxidation (acyl CoA dehydrogenase)
 uric acid formation (xanthine oxidase)
 electron transport in respiration chain
 Conezymatic form of vitamin B2 is FMN
Hypovitaminosis: disorders of the processes of biological oxidation symptoms include: cracks at the corner of the
mouth, dermatitis, and glossitis, Magenta tongue
reddening of oral mucosa, cracks on the lips and mouth corners, face skin dryness and desquamation,
conjunctiva inflammation, vasculature invasion into the cornea
Sources: Cereals, nuts, milk, eggs, green leafy vegetables and meat
Daily requirements: 1-3mg
32. Chemical and physiological name, coenzymes, biological role of vitamin B5. Manifestations of
hypovitaminosis, nature sources and day requirement of vitamin B5?
Vitamin В5 (pantothenic acid, anti-dermatitis)

Coenzymes:
 coenzyme А
 phosphopantothenate
Is necessary for the action of about 80 enzymes
Processes which are inhibited in vitamin В3 deficiency:

 oxidative de-carboxylation of pyruvate and alpha-ketoglutarate
 transport of the fatty acids residues
 synthesis of purine nucleotides
 activation of fatty acids
 phosphor-pantothenate is a constituent of multi-enzyme complex – fatty acids synthase
 cholesterol synthesis
 keto-genesis
Hypovitaminosis:
 dermatitis
 ulcers of mucosa
 spasms, paresis
 hypo-lipidemia
 liver steatosis
 absence of appetite, nausea, pain of stomach, diarrhea, head ache, disorders of memory
Daily requirement: 10-15 mg

Food: liver, eggs, fish, bread
Vitamin В3 (РР, nicotinic acid, nicotinamide niacin, anti-pellagric)
Nature: derivative of pyridine, Forms the coenzymes NAD and NADP

NAD and NADP – coenzymes of many оxidoreductases (oxidative reductive processes) NAD take part in:
 glycolisis
 gluconeogenesis
 PPC
 FA synthesis and
 oxidation
 AA deamination
 Krebs cycle (3 enzymes)
 ETC
 nucleic acids formation
NADP takes part in:

 FA synthesis
 cholesterol synthesis
Vitamin B3 takes part in CoASH formation
Hypovitaminosis: disease pellagra, dermatitis (exposed part of body), diarrhea, dementia
Causes of vitamin B3 hypovitaminosis:

 malabsorption
 alcoholism
 taking of cyto-statics and isoniazid for a long time
 protein starvation
 in persons who eat a lot of corn (lack of tryptophan from which В5 can be synthesized by bacteria)
Food: liver, meat, fish, black bread, yeast, eggs
Vitamin В6 (pyridoxine, аnti-dermatitic)
In the base of structure: pyridine core
Form coenzymes: pyridoxal phosphate carries chemical groups only (PLP), pyridoxamine and monophosphate (PMP)
PLP and PMP – coenzymes of enzymes of Amino acid metabolism:

 amino transferases
 aspartate aminotransferases
 decarboxylases
 participate in oxidation of amines
 synthesis of GABA inhibitor in CNS
Causes of Hypovitaminosis:
 in the using of antagonists (isoniazid, penicyllamine, L-DOPA, estrogens)
 in malabsorption, alcoholism
 increased requirement in pregnancy
Symptoms of hypovitaminosis:
 hyperaminoaciduria
 negative nitrogen balance
 dermatitis (erythema, pigmentation, edema)
 anemia (disorders of iron utilization)
 leucopenia (disorders of protein synthesis)
 growth inhibition
 convulsions, muscle spasms (GABA inhibition)
Avitaminosis of vitamin B6 causes a decreases in activity of transaminases in blood
Vitamin В10 (folic acid, anti-anemic)
In the base of structure: residue of pterine, para-amino benzoic acid, glutamic
Coenzyme: tetra-hydro folic acid (THFA)
Biological role of THFA: transfers methyl groups in the synthesis of amino acids, pyrimidine nucleotides, creatin and
methionine. In deficiency – disorders of the NA and protein synthesis, inhibition of growth and cell division
Symptoms:
 hyper chromic megaloblastic anemia treatment in combination of folic acid and Vitamin B12
 leucopenia
 thrombocytopenia
 glossitis, conjunctivitis, gastritis (disorders of epithelium proliferation)
 growth inhibition
 impairment of the wound healing
 immunodeficiency

Is formed by intestinal bacteria (large intestine), eukaryotic cells don’t synthesize folic acid
Food: bean, green leafy vegetables, clemons, mushrooms, meat and liver
Vitamin В12 (cyanocobalamin, аnti-anemic)

Structure: tetrapyrrol compound, Соbalt іоn, nucleotide part
Coenzymes: 5-deoxyadenosylcobalamin and меthyl cobalamin
Biological role:
 tightly connected to folic acid
 synthesis of methionine from homocysteine
 synthesis of creatin, choline
 synthesis of phospholipids
 synthesis of purine and pyrimidine bases, nucleic acids
Symptoms of avitaminosis:
 hyper chromic megaloblastic anemia (malignant, pernicious, Addison-Birmer disease)
 fatty dystrophy of nervous cells, neurological disorders
 cardiovascular disorders (accumulation of homocysteine)
Avitaminosis: can be caused by stomach resection – castle factor
Food source of vitamin B12: egg, meat, poultry and diary, Liver
Use Methylmalonic acid for diagnosis of vitamin B12
Daily requirement: 2-5µg
Is not synthesized neither in plants nor in animals. Is formed only by intestinal bacteria. It is absorbed in small
intestine
37. Chemical name, biological role of vitamin H. Manifestations of hypovitaminosis, nature sources and day
requirement of vitamin H?
Vitamin Н or B7 (biotin, anti-seborrheic)
Structure: consists of imidazole and thiophenone rings and Valerian acid
Coenzyme of carboxylase: serves as transporter of carboxylic group
 Pyruvate carboxylase in gluconeogenesis
 Acetyl-СоА carboxylase, propionyl-СоА carboxylase in lipid metabolism
 Biotin can bind CO2 and transport it
Hypovitaminosis almost does not occur can be in malabsorption, dis-bacteriosis, using of large amount of eggs white
which contains avidin (glycoprotein that irreversibly binds biotin – аnti-vitamin)
Symptoms of hypovitaminosis:
 seborrheic dermatitis of the hair part of head
 conjunctivitis
 anemia
 depression
Food: liver, soybeans, egg yolks, mushrooms, beans, onion, spinach
38. Chemical name, structure, active forms and properties of vitamins C. Biological role of vitamins C.
Manifestations of vitamins C hypovitaminosis. Nature sources and day requirement of vitamins C. Clinical
symptoms of vitamin P hypovitaminosis?
Vitamin С (L-ascorbic acid, аnti-scorbutic)
Structure – lacton of dienolgulonic acid
Coenzyme function: has not been established
Vitamin C has oxidation-reduction properties, can donate hydrogen, as result is converted to dehydroascorbic acid
Biological role of vitamin C:
 reduces sulfhydryl groups of proteins, enzymes
 formation of serotonin
 synthesis of norepinephrine
 synthesis of steroid hormones
 formation of carnitine
 synthesis of collagen (hydroxyl proline) – hydroxylation pf proline
 formation of THFA
 decomposition of hemoglobin
 Fe3+ ® Fe2+ - absorption in the intestine
 promote immunity defense
 required for synthesis of bile acids, collagen, epinephrine, intestinal absorption of iron
Vitamin C Hypovitaminosis scurvy:

 hemorrhages, loose of teeth, gums swell and bleed easily (collagen deficit)
 anemia (lack of THFA)
 pain in heart, swelling of legs, weakness, fatigue
 loss of weight
 Petechial
Note: Xeropthalmia is not a symptom of Scurvy
Hypovitaminosis of Vit. C can develop in carnivorous person
An early diagnosis of vitamin C deficiency by measuring plasma, urinary and ascorbic acid saturation
Daily requirement: 80-100mg or 75-100 mg, Requirement is increased in infections, flue, in pregnancy
Food: Citrus fruit,
Vitamin Р (bioflavonoids, factor of permeability)

Biological role of vitamin P:
 synergist of vitamin C (used in ascorutin preperations prevents scurvey)
 protects vitamin C against oxidation
 hydroxylation of proline and lysine
 inhibit hyaluronidase
 prevent oxidation of epinephrine
 antioxidants
Hypovitaminosis of vitamin P:
 petechial: is a small (1–2 mm) red or purple spot on the skin, caused by a minor bleed from broken capillary
blood vessels
 symptoms of scurvy
20-30mg excreted in urine
Food: pepper, citrus, black currant, rowan, buckwheat, fruits
39. Common properties of fat soluble vitamins. The differences of fat soluble vitamins from water soluble
vitamins?
Water soluble Vitamins Fat soluble Vitamin

Form Coenzymes Do not form coenzymes
Do not effect membranes Modulator of membranes
Do not have anti-oxidant properties except vitamin C Most are antioxidant
Do not effect genetic apparatus Causes the expression of genes
Do not cause hypervitaminosis Cause hyper-vitaminosis
Do not have provitamins Have provitamins
Requires bile acids and fats for absorption
Not component of enzymes
40. Chemical and physiological name, structure and provitamins of vitamin A. Biological role of vitamins A.
Clinical symptoms of vitamin A hypovitaminosis and hypervitaminosis. Nature sources and day requirement
of vitamins A?
Vitamin А: Retinol, Antixerophthalmic (inhibit pathologic drying of the conjunctiva)
Active forms: Retinol, Retinal, Retinoic acid
Precursors/Provitamin: carotenoids most important is Beta carotene which is cleaved to retinol in the liver
Biological functions of vitamin A

 Modulator of bio membranes: changes the permeability, synthesis of membranes components
 Growth vitamin: stimulates the synthesis of proteins (especially in cartilages), stimulates the synthesis of
purine and pyrimidine nucleotides
 Participates in oxidation-reduction reactions
 Regulates the synthesis of keratin (prevents the conversion of cylindrical epithelium into horny)
 Promotes the spermatogenesis and placenta development
 Stimulates the synthesis of antibodies and phagocytosis (anti infectious)
 Regulates the hormonal status: prevents the oxidation of vitamin C, inhibits the synthesis of thyroxin
 Maintains the antioxidant potential of different tissues
 Vitamin A is responsible for the vision cycle
 To maintain the integrity of epithelial tissue
Hypovitaminosis Hypervitaminosis
Night blindness- prolonged dark adaptation time Accumulates in liver
Anemia (vit. A is required for the synthesis of vomiting, diarrhea
transferrin)
Increased susceptibility to infection and cancer liver and spleen enlargement
Follicular hyperkeratosis (“goosebumps” skin)
Xerophthalmia (progressive keratinization of cornea) loss of hair
Keratomalacia (corneal ulcerations) dermatitis
pyelonephritis (change of endothelium in nephrons)
Twilight vision impairment

Vitamin A sources: includes animal sources such as eggs, meat and diary
Beta carotene sources (precursor of vitamin A): include green leafy vegetables and intensely colored fruits and
vegetables
41. Chemical and physiological name, structure and provitamins of vitamin D. Biological role of vitamins D.
Clinical symptoms of vitamin D hypovitaminosis. Nature sources and day requirement of vitamin D and
hypervitaminosis?
Vitamin D: (cholecalciferol, аntirickets)
Two forms of vitamin D: Vitamin D2 (ergocalciferol) and Vitamin D3 (cholecalciferol), both of them are metabolized
by the liver
Parathyroid hormone stimulates the formation of 1,25- dihydroxycholecalciferol in kidneys
Pro vitamin of D3 is 7-dehydrocholesterol
Active form is Calcitriol (1,25- dihydroxycholecalciferol)
Deficiency: rickets and osteomalacia
Functions of vitamin D:
 regulates the Ca and P levels in the blood and it acts in concert with parathyroid hormone
 promotes absorption of Ca and P in the intestine
 promotes reabsorption of Ca in the kidneys
 high levels of serum Ca and P increase the rate of bone mineralization
 promote bone resorption (at low Ca in blood)
 promotes phagocytosis
 immunomodulatory activity
 induces differentiation of immune cells
 stimulates the formation of 1,25- dihydroxycholecalciferol in kidneys
 dysfunctional parathyroid leads to spasm development
 prevents tumor genesis
o inhibits proliferation
o inhibits angiogenesis
o induces differentiation
 Activates reabsorption of amino acids, especially proline
 Activates the monosaccharides phosphorylation (glycogen synthesis)
 Promotes ATP formation
 Causes: Hypercalciemia, hypophosphatemia and the intensive excretion of phosphorus with urine
 Hypocalciemia, hyperphosphatemia and decreased excretion of phosphorus with urine were found. It can be
caused by: Decreased production of parathormone
Hypo-vitaminosis Hyper-vitaminosis
Increase of Ca and P in blood
Richkets: softening of bone symptoms include: muscle Demineralization of bones
weakness, Tetany, deformed skeletal bones i.e. bowed Calcification of inner organs
legs, Dental problems, fractures and hypocalcemia Renal stones
Daily Requirements: 12-25µg

Sources: sunlight, dairy and fish
42. Chemical and physiological name, biological role of vitamin E. Clinical symptoms of vitamin E
hypovitaminosis. Nature sources and day requirement of vitamin E and hypervitaminosis?
Vitamin E: Tocopherols and tocotrienols. Antisterile:

Group of tocopherols and tocotrienols, most active is alpha-tocopherol
Biological role of vitamin E
 Most potent antioxidant
 Active scavenger of free oxygen and nitrogen radicals
 Protects vitamin A from oxidation
 Prevents oxidation of Se
 Stabilizes the cell membranes
 Increases the resistance of membranes to oxidation and toxic effects
 Improves cellular respiration stabilizing ubiquinone
 Prevents oxidation of LDL
 Reduces risk of atherosclerosis
 Regulates transcription
 Maintains normal immune function
 Inhibits cholesterol biosynthesis
 Stimulates mobilization of Ca from bones has nothing to do with its antioxidative properties
Hypovitaminosis of vitamin E is caused by: malabsorption and famine and symptoms include:
 Activation of FRO
 Increase of membrane permeability
 Hemolysis of erythrocytes
 Deficit of ATP
 Muscle dystrophy (creatinuria)
 Demyelization of nerves (CNS changes)
 Disorders of reproductive function (atrophy of testis, azoospermia, inability to implantation)

Food sources: corn, nuts, olives, green leafy vegetable oils
43. Chemical and physiological name, biological role of vitamin K. Clinical symptoms of vitamin K hypovitaminosis
and hypervitaminosis. Nature sources and day requirement of vitamin K. Chemical and physiological name,
biological role of vitamin F. Nature sources and day requirement of vitamin F.
Vitamin K Quinone derivatives Anti-hemorrhagic

 K1, phyloquinone (in green vegetables)
 K2, menaquinone (is synthesized by intestinal bacteria)
 Vikasol is a synthetic analogue of vitamin K
Biological functions of vitamin K
•Stimulates the synthesis of coagulation factors in liver
•Increases the resistance of capillaries
•Stimulates the synthesis of albumins, pepsin, trypsin, lipase, amylase
•Increases the peristalsis of intestine
•Inhibits free radical oxidation
 Vitamin K is involved in posttranslational modification of the blood clotting factors by acting as cofactor for
the enzyme Decarboxylase
Hypovitaminosis of vitamin K
Causes by:
 Lipids malabsorption (lack of bile acids)
 Disbacteriosis (vitamin K is synthesized by intestinal microflora)
 Taking of antivitamins (dicumarol)
Lack of red meat does not cause vitamin K deficiency
Lack of vitamin K causes: Kakheksiya
Symptoms:
 Hemorrhages (subcutaneous, intramuscular, into inner organs)
 Increased coagulation time
Daily requirement: 0.2-0.3 mg
Food source of vitamin K: cabbage, cauliflower and spinach
Vitamin F Polyunsaturated fatty acids Antisclerotic

 Linoleic acid
 Linolenic acid
 Arachidonic acid
Biological functions of vitamin F

 Participate in the organism growth and development
 Components of phospholipids (cell membranes)
 Regeneration of skin epithelium
 Synthesis of prostaglandins (20 C)
 Decrease cholesterol level
 Increase the organism resistance
Hypovitaminosis of vitamin F
Causes/ symptoms:
 Growth retardation
 Dermatitis
 Dry skin
 Eczema
 Atherosclerosis
Daily requirement: 10-15g
44. The blood functions, their characteristic. Biochemistry of blood cells. Function of leucocytes?
Functions of blood
1.Transport:
transport of oxygen and carbon dioxide
transport of nutrients and products ofmetabolism
2. Osmotic.
3. Regulatory (formation of hormonoids).
4. Protective.
5. Detoxification.
6. Thermoregulatory.
Blood composition: 6-8% of total body weight

55% Plasma 7% proteins Proteins include
91.5% water
54% Albumin
1% other solutes e.g. gases,
38% Globular protein
metabolic wastes and nutrients
7% fibrinogen
1% other
11
45% Blood formed elements Platelets 1.5-4*10 /L White blood cells
60-70% Neutrophils
20-25% Lymphocytes
3-8% Monocytes
2-4% Eosinophils
0.5-1% Basophils
Physical properties of Blood:

 pH: 7.35-7.45
 Viscosity: 3-4 centipoise
 Specific gravity: 1.056-1.066
Leukocytes
Unit Neutrophils Basophils Eosinophils Lymphocytes Monocyte

Young Stab/ Segmenta
Rod l
Relative 0-1% 1-6% 47-72% 0-1% 0.05-5% 18-37% 3-11%
%
0-0.01 0.01- 0.47-0.72 0-0.01 0.005-0.05 0.18-0.37 0.03-0.11
0.06
Absolute 0.006 0.06- 2.82-4.32 0-0.06 0.03-0.3 1.08-2.22 0.18-0.66
(i.e. *6) 0.36
Functions of Leukocytes and erythrocytes :

Basophils allergic reactions, blood clotting,
Produce a lot of histamine, serotonin, heparin (polysaccharide anticoagulant)
Energy mainly from oxidative phosphorylation
Eosinophils protection from microorganisms, allergic reactions.
Amount is increased in helminthosis, organism sensibilization, allergy
Lymphocytes formation of humoral and cell immunity. Intensive synthesis of protein - immunoglobulins
Т and В lymphocytes
Energy mainly from glycolysis
Monocyte phagocytosis, exit into tissues and formstissue macrophages
have a lot of lysosomal hydrolases
Aerobic pathway of energy obtaining prevails
Thrombocyte Function: formation of blood clot
2 types of granules:
 dense (АТP, serotonin, catecholamines);
 аlpha-granules – lysosomes
Main reactions: adhesion, aggregation, secretion
Synthesize: actin, myosin, troponin, prostaglandins and thromboxans
Erythrocytes Function: transport of gases
Do not contain nucleus and mitochondria
Main protein: hemoglobin (35 %)
Energy: from glycolisis
Formation is stimulated by erythropoetin
45. Respiratory function of erythrocytes. Structure and biological role of hemoglobin. Types of hemoglobin?
Erythrocyte functions: erythrocytes are dedicated to respiratory gas transport. Hemoglobin reversibly binds with
oxygen and most oxygen in the blood is bound to hemoglobin. Erythrocytes do not contain nucleus and mitochondria
Main protein – hemoglobin (35 %) Energy – from glycolysis Life span – 120 days Formation is stimulated by
erythropoetin
Normal level of hemoglobin (Hb) in blood in males is 14–16 g/dl and in females, 13–15 g/dl.
Hb is globular in shape
Hemoglobin type structure %

adult Hb (HbA) 2 alpha chains and 2 beta chains 97
Hb F (fetal Hb) of 2 alpha and 2 gamma chains 1
Hb A2 2 alpha and 2 delta chains. 2
STRUCTURE OF HEMOGLOBIN
Hemoglobin is a porphyrin containing compound, it’s a tetramer made up of 4 subunits where each subunit is
contains a heme group (prosthetic group) and a polypeptide chain. It has tertiary protein structure. The 4
polypeptide chains are held by disulfide bridges
46. Structure and biological role of hemoglobin. Types of hemoglobin. Pathological hemoglobin’s. Derivatives of
hemoglobin, conditions of their appearance?
Hemoglobin Derivatives:
Oxyhemoglobin oxy-Hb bright red substance formed by the combination of haemoglobin with oxygen,
present in oxygenated blood.
Deoxyhemoglobin Deoxy-Hb Hb without oxygen
Methemoglobin Met-Hb Fe3+ instead of Fe2+ in heme group, can be due to congenital disease, drugs such as
benzocaine, aniline dyes
Carbonyl hemoglobin HbCO CO binds to Fe2+ in heme in the case of CO poisoning. CO has X200 the affinity to Fe 2+
than oxygen
Carbaminohemoglobin CO2 is non covalently bound to globin chain of hemoglobin
HbCO2
Hemichromes Hemichromes are typically produced by the slow denaturation of methemoglobin
Ferritin High levels of ferritin can indicate an iron storage disorder, such as hemochromatosis,
or a chronic disease process. Low levels of ferritin are indicative of iron deficiency,
which causes anemia
Hemosidirin a yellowish brown granular pigment formed by breakdown of hemoglobin, found in
phagocytes and in tissues especially in disturbances of iron metabolism (as in
hemochromatosis, hemosiderosis, or some anemias)
Thalassemias are inherited blood disorders characterized by abnormal hemoglobin production. The thalassemias are
classified according to which chain of the hemoglobin molecule is affected. In α-thalassemias, production of the α
globin chain is affected, while in β-thalassemia, production of the β globin chain is affected.
 α-thalassemias involve the genes HBA1[26] and HBA2,[27] inherited in a Mendelian recessive fashion
 Beta thalassemias are due to mutations in the HBB gene on chromosome 11,[28] also inherited in an
autosomal, recessive fashion.
 Delta-thalassemia
Hemoglobin E or haemoglobin E (HbE) is an abnormal hemoglobin with a single point mutation in the β chain
Hemoglobin c (abbreviated as Hb C or HbC) is an abnormal hemoglobin in which substitution of a glutamic acid
residue with a lysine residue at the 6th position of the β-globin chain has occurred
Hemoglobin D caused by substitution of glutamine instead of glutamate
Hemoglobin S (Hgb S) is an abnormal type of hemoglobin that you can inherit from your parents. Hgb S causes red
blood cells to become stiff and abnormally shaped. Instead of having a normal round, disk shape, these red blood
cells become sickle-shaped,
47. The total contents of proteins in blood plasma.The main proteins of blood plasma. Causes and consequences
of hyperproteinemia and hypoproteinemia?
Possible causes of high blood protein include I.e. hyperproteinemia:
 Amyloidosis (buildup of abnormal proteins in your organs)
 Dehydration.
 Hepatitis B.
 Hepatitis C.
 HIV/AIDS.
 Monoclonal gammopathy of undetermined significance (MGUS)
 Multiple myeloma.
Causes of hypoproteinemia:
 Celiac disease
 Poor diet (not enough calories) – not enough protein consumption
 Liver disorder
 Kidney problems i.e. pissing away proteins
 Inflammatory bowel disease
48. Albumins: content in blood plasma, physical and chemical properties.Functions of albumins?
Serum albumin concentration is typically 35 - 50 g/L (60% of plasma content)
Functions of albumin:
 Maintains oncotic pressure
 Transports thyroid hormones
 Transports other hormones, in particular, ones that are fat-soluble
 Transports fatty acids ("free" fatty acids) to the liver and to myocytes for utilization of energy
 Transports unconjugated bilirubin
 Transports many drugs; serum albumin levels can affect the half-life of drugs
 Competitively binds calcium ions (Ca2+)
 Serum albumin, as a negative acute-phase protein, is down-regulated in inflammatory states. As such, it is
not a valid marker of nutritional status; rather, it is a marker of an inflammatory state
 Prevents photodegradation of folic acid
49. Globulins: content in blood plasma, physical and chemical properties.Functions of globulins?
Globulins are produced by liver and by plasma cells, which develop from B lymphocytes. Antibodies
(immunoglobulins- glycoproteins)) help attack viruses and bacteria. Alpha and beta globulins transport iron, lipids,
and fat-soluble vitamins.
 Alpha 1 Globulin: antitrypsin, alpha lipoproteins
 Alpha 2 globulins: Caeruloplasminn (copper carrying protein in blood, deficiency leads to Wilson disease),
heptoglobins (acute-phase reactant whose principal clinical utility is in defining conditions of hemolysis.
levels can also become elevated in infection and inflammation), alpha 2 macroglobulin
 Beta globulins: beta lipoproteins, transferrin (Transferrins are iron-binding blood plasma glycoproteins that
control the level of free iron), fibrinogen
 Gamma globulins: immunoglobulins, CRP
 E and D globulins: not synthesized in liver
IgA provides highest antiviral activity – its secretory
50. LDL and HDL as the principal transport forms of cholesterol.The direction of the cholesterol transport by LDL
and HDL. The principle of percentage ratio determination of LDL and HDL in blood serum, usage of this index
in atherosclerosis pathogenesis.
51. Liver’s functions. Role of liver in?

1. Bile Secretion and synthesis: required for absorption and emulsionof dietary fats
2. Carbohydrate Metabolism: maintain blood glucose level by breaking down glycogen to glucose and
releasing it to the blood when blood glucose level is low. The liver can also convert certain amino
acids, lactic acids and other sugars such as fructose and galactose to glucose. When blood glucose
level is high, the liver converts glucose to glycogen and triglycerides for storage.
3. Lipid Metabolism: hepatocytes store some triglycerides, break down fatty acids to generate ATO,
synthesize lipoproteins which transport fatty acids, triglycerides and cholesterol to and from body
cells. Liver also synthesize cholesterol and use cholesterol to make bile salts
4. Protein Metabolism: hepatocytes deaminate (remove the amino group NH 2) from amino acids so
that the amino acids can be used for ATP production or converted to carbohydrates or fats. The
resulting toxic ammonia (NH3) is then converted into the much less toxic urea which is excreted in
urine. Hepatocytes also synthesize most plasma proteins such as alpha and beta globulins,
prothrombin and fibrinogen
5. Processing of drugs and hormones: the liver can detoxify substances such as alcohol and excrete
drugs such as penicillin and sulfonamides into bile. It can also chemically alter or excrete thyroid
hormones and steroid hormones such as testosterone and aldosterone
6. Excretion of bilirubin: bilirubin is derived from heme of aged red blood cells and is absorbed by the liver
from blood and secreted into bile. Most of the bilirubin in bile is metabolized in the small intestine by
bacteria and eliminated in feces.
7. Storage: liver is a prime storage site for vitamin A, B12, D, E and K and minerals such as iron and copper
which are released from the liver when needed elsewhere in the body
8. Phagocytosis: Kupffer cells of the liver phagocytose aged red blood cells, white blood cells and some
bacteria
9. Activation of vitamin D: the skin, liver and kidney participate in synthesizing the active form of vitamin
D
52. carbohydrate metabolism?
 glycolisis
 metabolism of fructose and galactose
 gluconeogenesis (from amino acids and glycerine)
 release of glucose into blood (maintain the stable glucose concentration in blood)
 conversion of pyruvate into acetyl CoA
 tricarboxylic acid cycle
 pentose phosphate pathway NADPH2/ NADPH and pentose synthesis)
 glycogenolysis, glycogenogenesis
53. lipid metabolism?
 Synthesis of lipoproteins
 Synthesis of triacylglycerol’s
 Synthesis of phospholipids
 Synthesis of fatty acids, elongation of fatty acids chain, desaturation
 Synthesis of cholesterol
 Ketone bodies formation (from acetyl CoA in mitochondria of livercatalse)
 Lipolysis
 Fatty acids oxidation
54. protein metabolism?
 Protein synthesis, including blood plasma proteins

 Protein decomposition; urea synthesis (using enzyme Carbomoyl phosphate synthase – liver enzyme)
 Conversion of proteins into carbs and lipids
 Interconversion of amino acids
 Conversion of proteins into low molecular weight nitrogen containing substances
55. Liver’s functions. Role of liver in regulation of vitamin metabolism and water-salts balance?
Vitamin Metabolism:
 Formation of active form of vitamin D
 Formation of vitamin A from carotenes
 Depo of cyanocobalamin (synthetic form of vitamin B12) and folic acid
 Depo of vitamin E
 Phosphorylation of vitamins B, formation of coenzyme forms
Albumin helps in maintaining osmolarity and liver also produces Angiotensin which is involved in water salt balance
of the body i.e. Renin, Angiotensin, Aldosterone system, lack of albumin leads to edema/edemata
56. Liver’s functions. Role of liver in secretion of bile. The decomposition of hemoglobin in tissues, bile pigments
formation.
Main functions of liver:
1. Metabolism: anabolism and catabolism
2. Storage of nutrients: carbohydrates and fats can be stored as glycogen (polysaccharide), lipoprotein or as
triglycerides. Proteins are not stored in liver but are processed into molecules like albumin and are released
into the blood stream
3. Detoxification: modifying toxins so they can’t hurt our body. This is achieved mainly by Cytochrome P450
enzymes (induces conjugation via inductor of the synthesis of UDP-glucuronyltransferase, contains Feci)
4. Bile Production: bile is needed for absorption of fats from our foods.
5. Depot of iron and vitamins
Bile: bile is a digestive juice that is produced in the liver and stored in the gall bladder. Composition of bile in the gall
bladder is 97% water, 0.7% bile salts/acids which are amphiphilic steroids that emulsify ingested fats e.g. cholic acid,
DeoxyCholic acid and Tauracholic acid, 0.2% Bile pigments i.e. break down products of hemoglobin e.g. bilirubin,
0.5% fats (cholesterol, fatty acids and lecithin)
Bile pigment formation i.e. bilirubin: Red blood cells have a life span of roughly 120 days and then gets destroyed in
the spleen and the liver by macrophages. This releases the hemoglobin component which is then split into the heme
and globin component. The globin is further split into amino acids and recycled in the body. The heme is then split
into iron and Biliverdin. The Biliverdin is then converted into unconjugated bilirubin (non-water soluble) by the
enzyme Biliverdin Ruductase. The conjugated Bilirubin is transported to the liver with albumin as a carrier protein
where it is converted to conjugated Bilirubin (i.e. water soluble form). This is achieved with the combination of
Glucuronic acid with unconjugated Bilirubin.
The conjugated Bilirubin is then transported through the biliary channels to the duodenum. In the colon the bilirubin
is converted to urobilinogen and stercobilinogen and these are secreted as Stercobilin.
57. Kinds of jaundice, short description?
Classification of Jaundice
Class of Jaundice Types of Bilirubin increase Causes
Pre-hepatic or Unconjugated / indirect Abnormal red blood cells; antibodies; drugs and toxins;
hemolytic thalassemia; hemoglobinopathies, deficiency of UDP-
glucuronyltransferase, immune hemolytic anemia
Hepatic or Unconjugated and Viral hepatitis, toxic hepatitis, intrahepatic cholestasis
hepatocellular conjugated
Post-hepatic/ Conjugated/direct or and Gallstones (made from cholesterol), tumors of bile duct or
Mechanical / unconjugated/ indirect pancreas
obstructive
Liver function can be tested with measurement of bilirubin in serum and urobilinogen in urine.
 Normal serum bilirubin: 0.2-0.6mg/dl
 Normal Conjugated bilirubin: 0-0.2mg/dl
 A rise in serum bilirubin above 1 mg/dl is abnormal (latent jaundice) but jaundice only appear if level is
above 2mg/dl
58. Kidney functions in organism?

Functions of the kidneys:
1. Regulation of blood ionic composition: the kidneys help regulate the blood levels of several ions most
importantly sodium, potassium, calcium, chloride and phosphate ions
2. Regulation of blood pH: the kidneys excrete a variable amount of H+ into the urine and conserve
bicarbonates ions which is an important buffer in pH of blood. This help in regulating blood pH
3. Regulation of blood volume: the kidneys adjust blood volume by conserving or eliminating water in urine.
An increase in blood volume increases blood pressure while a decrease in blood volume decreases blood
pressure.
4. Regulation of blood pressure: the kidneys also help regulate blood pressure br secreting enzyme Renin
which activates the Renin-Angiotensin-Aldosterone pathway. Increased Renin causes an increased blood
pressure
5. Maintenance of blood osmolarity: by separately regulating loss of water and loss of solutes in urine the
kidneys maintain a relatively constant blood osmolarity close to 300millimol/liter (mOsm.Litre)
6. Production of hormones: the kidney produces three hormones :
a. Erythropoietin: produced by peritubular capillary endothelial cells in response to hypoxia and it
stimulates the bone marrow in red blood cell production
b. Renin: produced by Juxtaglomular apparatus of kidney due to decrease arterial pressure or sodium
chloride content in blood. Renin plays an important role in conversion of angiotensin to angiotensin I
c. Calcitriol: the active form of vitamin D, stimulates calcium absorption in the intestine and calcium
and phosphate reabsorption in the kidneys
7. Regulation of blood glucose level: like the liver, the kidney can use amino acid Glutamine in Gluconeogenesis
for the synthesis of glucose during starvation
8. Excretion of wastes and foreign substances: by forming urine, the kidneys help in excreting wastes such as
ammonia and urea from deamination of amino acids. Bilirubin from the catabolism of hemoglobin, creatinine
from creatine phosphate break down in muscle fibers. Uric acid from catabolism of nucleic acid. Drugs etc..
59. Physical and chemical characteristics and components of urine: a) volume, physical and chemical properties
of urine; b) inorganic components of urine; c) organic components of urine?
Properties of urine:
1. Amount: 1500-2000mL/day
1. Polyuria: caused by diabetes mellitus (high osmotic pressure of urine) and insipidus (insufficient
ADH)
2. Oliguria: heart failure, nephritis, vomiting , fever
3. Anuria: due to kidney failure, acute intoxication by heavy metals
2. Color: straw-yellow
1. if pale then its Polyuria (diabetes insipidus)
2. if dark then its jaundice (concentrated urine)
3. if red then there is blood in it
4. Green blue: decay of proteins in the intestine (Conjugation with sulphuric and glucuronic acids)
3. Urine should be transparent if cloudy there is pus or mucin in urine due to:
1. Metabolic disorders
4. Density: 1.012-1.020g/mL
1. Increased density: increase in organic/ inorganic substances due to e.g. diabetes mellitus
2. Decreased density: can be caused by diabetes insipidus
5. pH: 5.5-6.8
1. Acidic: due to diabetes mellitus, starvation, fever and meat consumption
2. Alkaline: die to Cystitis, Pyelitis and consumption of plants
6. Isostenuria: continuously low density in oliguria (kidney failure) – index for lack of Anti diuretic hormone
60. Pathological components of urine, which appear due to different metabolic disorders in organism?
Hematuria: caused by the presence of blood cells in urine, it can be:

1. Macrohematuria: can be seen by eye
2. Microhematuria: need a microscope to see the blood
Causes of hematuria
 Infectious diseases: glomerulonephritis, pyelonephritis, prostatitis, urethritis, cystitis
 stones in kidneys and urinary tracts
 Trauma of kidneys and organs of urinary tracts
 Tumors of kidneys and organs of urinary tracts: cancer of kidneys, bladder
Glycosuria: glucose can be in urine for physiological and pathological reasons:

 Physiological: 30-60minutes after carbohydrate consumption or emotional stress
 Pathological:
o Related to Hyperglycemia: Insulin deficit i.e. Diabetes mellitus or pancreatitis, Extrainsular: e.g.
disorders of thyroid gland, pituitary and liver disease
o Not related to hyperglycemia: renal glycosuria/ renal diabetes (normal glucose level in blood)
Bilirubinuria / Bilirubinglucoronids (beer color of urine): appearance of bilirubin in urine as a result of

conjugated/direct bilirubin in blood, causes of this is mechanical and parenchymal jaundice -
Urobilinuria (brown color in urine): caused by overburdening the liver, excessive RNC breakdown, hepatic infection,
liver cirrhosis and increased urobilinogen production
Phenylketonuria (phenyl pyruvate in urine): a genetic disease caused due to the absence or deficiency of
phenylalanine 4 hydroxylase, diagnosed with FeCl3
Pyuria (cloudy urine): condition where there is pus or too many white blood cells in urine. Causes include:
 Infectious causes: tuberculosis and infection of prostate
 Noninfectious causes: treatment of glucocorticoids, mechanical trauma, kidney stones and tumors
Hemolytic mechanical Hepatic

Bilirubin - + +
Urobilin + - +
Amino acid phenylalanine forms benzoic acid in tissues which is then interacts with glycine and detoxified in liver to
hippuric acids which is excreted in urine
Activity of alanine amino peptidase is tested for in urine to check for acute kidney inflammation
Proteinuria: presence of protein in urine
Proteinuria Type Pathophysiological features cause
Glomerular Increased glomerular capillary Primary or secondary
permeability to protein glomerulopathy
Tubular Decreased tubular reabsorption of Tubular or intestinal disease
proteins in glomerular filtrate
Overflow Increased production of low Monoclonal gammpathy, Leukeia
molecular weight proteins
61. General description of connective tissue. Structure and functions of collagen. Elastin–main protein of elastic
fibrils, structure and biological role?
As the name implies, connective tissue serves a connecting function. It supports and binds other tissues in the body.
Unlike epithelial tissue, which has cells that are closely packed together, connective tissue typically has cells scattered
throughout an extracellular matrix of fibrous proteins and glycoproteins attached to a basement membrane. The
primary elements of connective tissue include a ground substance, fibers, and cells.
The ground substance acts as a fluid matrix that suspends the cells and fibers within the particular connective tissue
type. Connective tissue fibers and matrix are synthesized by specialized cells called fibroblasts. There are three main
groups of connective tissues: loose connective tissue, dense connective tissue, and specialized connective tissue.
Loose Connective Tissue

In vertebrates, the most common type of connective tissue is loose connective tissue. It holds organs in place and
attaches epithelial tissue to other underlying tissues. Loose connective tissue is named so because of the "weave"
and type of its constituent fibers. These fibers form an irregular network with spaces between the fibers. The spaces
are filled with ground substance. The three main types of loose connective fibers include collagenous, elastic, and
reticular fibers.
Collagenous fibers are made of collagen and consist of bundles of fibrils that are coils of collagen molecules. These
fibers help to strengthen connective tissue.
Elastic fibers are made of the protein elastin and are stretchable. They help to give connective tissue elasticity.
Reticular fibers join connective tissues to other tissues.
Loose connective tissues provide support, flexibility, and strength required to support internal organs and structures
such as blood vessels, lymph vessels, and nerves.
Dense Connective Tissue

Another type of connective tissue is dense or fibrous connective tissue, which can be found in tendons and
ligaments. These structures help attach muscles to bones and link bones together at joints. Dense connective tissue is
composed of large amounts of closely packed collagenous fibers. In comparison to loose connective tissue, dense
tissue has a higher proportion of collagenous fibers to ground substance. It is thicker and stronger than loose
connective tissue and forms a protective capsule layer around organs such as the liver and kidneys.
Dense connective tissue can be categorized into dense regular, dense irregular, and elastic connective tissues.
Dense regular: Tendons and ligaments are examples of dense regular connective tissue.
Dense irregular: Much of the dermis layer of the skin is composed of dense irregular connective tissue. The
membrane capsule surrounding several organs is also dense irregular tissue.
Elastic: These tissues enable stretching in structures such as arteries, vocal cords, the trachea, and bronchial tubes in
the lungs.
Specialized Connective Tissues
Specialized connective tissues include a number of different tissues with specialized cells and unique ground
substances.
Some of these tissues are solid and strong, while others are fluid and flexible.
Adipose
Adipose tissue is a form of loose connective tissue that stores fat. Adipose lines organs and body cavities to protect
organs and insulate the body against heat loss. Adipose tissue also produces endocrine hormones.
Cartilage
Cartilage is a form of fibrous connective tissue that is composed of closely packed collagenous fibers in a rubbery
gelatinous substance called chondrin. The skeletons of sharks and human embryos are composed of cartilage.
Cartilage also provides flexible support for certain structures in adult humans including the nose, trachea, and ears.
Bone
Bone is a type of mineralized connective tissue that contains collagen and calcium phosphate, a mineral crystal.
Calcium phosphate gives bone its firmness.
Blood
Interestingly enough, blood is considered to be a type of connective tissue. Even though it has a different function in
comparison to other connective tissues, it does have an extracellular matrix. The matrix consists of the plasma with
red blood cells, white blood cells, and platelets suspended in the plasma.
Lymph
Lymph is another type of fluid connective tissue. This clear fluid originates from blood plasma that exits blood vessels
at capillary beds. A component of the lymphatic system, lymph contains immune system cells that protect the body
against pathogens.
COLLAGEN
See Figure 6–4 for collagen structure and Figure 6–5 for collagen synthesis.
■ 1/3 of body’s protein.
■ Consists of three polypeptide a-chains wound around one another to form
a triple helix.
■ Produced by many cells: fibroblasts, epithelial cells, odontoblasts, osteoblasts,
and chondrocytes.
■ It is the organic matrix in dentin and cementum
■ 35% glycine; 21% proline; 11% alanine.
■ Fibers have high tensile strength.
COLLAGEN SYNTHESIS
■ Intracellular events
■ rER: Synthesis of a-chains with glycine-x-y sequence.
■ rER: Hydroxylation of proline and lysine residues, forming hydroxyl proline and hydroxylysine. Requires vitamin C.
■ Golgi: Glycosylation of α-chains, forming procollagen, a triple helix containing N- and C-terminal propeptides.
■ Extracellular events
■ Endopeptidases cleave the N- and C-terminal propeptides of procollagen, forming tropocollagen.
■ Cross-linking of tropocollagen molecules, forming collagen fibrils.
Requires oxidation of lysine via lysine oxidase (contains copper).
Types of Collagen
Type Location
I Skin, bone, tendon, sclera, dentin, cementum, gingiva, PDL
II Cartilage, vitreous humor
III Embryonic CT, organ CT, blood vessels, pulp, PDL
IV Basement membrane
V Widely distributed CT, dentin, gingiva, PDL
VII Anchoring fibrils of basement membrane
ELASTIN
■ Fibers are extremely elastic, “rubber-like.”
■ Found in skin, ligaments, arterial walls.
■ Synthesis can occur simultaneously with collagen.
■ Synthesized similarly to collagen:
■ Amino acid sequence of the proelastin polypeptide chain is typically glycine-x-y. Other residues include
proline, lysine, alanine, and hydroxyproline (to a lesser extent).
■ Endopeptidases cleave the N- and C-terminal propeptides of proelastin, forming tropoelastin.
■ Cross-linking of tropoelastin molecules via desmosine, forming elastin fibers. Requires oxidation of lysine
via lysine oxidase (contains copper).

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1. Enzymes (concept). Common properties of enzymes and inorganic catalysts.

The specific properties of

Similarities and Differences between enzymes and catalysts

Cofactor may be:

Six classes of enzymes according to mechanism of action

Zymogens are activated by proteolytic activation

Coenzymes: non protein portion of an enzymes

An enzyme can be:

3. Characteristic of thermolability and specificity of enzyme action?

4. The effect of pH on enzyme activity. Optimal pH for different enzymes?

Enzymes pH Optimum Enzymes pH Optimum

5. Active sites and allosteric site of enzymes?

6. The origin of blood enzymes. Enzymes specific to different organs:

Central intermediate product of metabolism is: Acetyl-CoA

Functions of Citric acid cycle:

Citric acids Cycle overall reaction:

Citric acids Cycle:

Process Location Phosphorylation Net ATP per Glucose

9. What is macroergic bond? Examples of high energy compounds?

Energy released by high energy phosphate reactions Reaction ΔG [kJ/mol]

Ways of ATP formation:

Process Location Phosphorylation Net ATP per Glucose

ATP production per Molecule of glucose

Note: NADH yields 3 ATP and FADH2 yields 2 ATP

12. Digestion of carbohydrates: localization, types, role of enzymes?

14. Diabetes mellitus: types, causes, disorders of metabolism, symptoms, treatment?

Diabetic tendency can be detected by the glucose-tolerance test.

Steroid diabetes: high level of 17-ketosteroids in urine

16. Biological role of cholesterol. Contents of cholesterol in blood, transport forms?

Cholesterol chart for adults

Total cholesterol HDL cholesterol LDL cholesterol Triglycerides

Borderline 200–239 n/a 130–159 150–199

High 240 or higher n/a 160 or higher 200 or higher

Low n/a less than 40 n/a n/a

Released free cholesterol:

Biological role of proteins

The general ways of amino acids degradation:

Deamination of amino acids

There are different transaminases, T h e most common:

Decarboxylation of amino acids

Significance of amino acid decarboxylation

20. Hormones as biological regulators. Hormonoids (histohormones). Endocrine glands. Classification of

Specific stimulus for hormones secretion is:

Classification of hormones according to chemical nature:

The Final effect of hormones

Chemical nature: simple protein

Carbohydrate Protein Lipid

Adrenocorticotropic hormone (АCTH)

Controls the cortex of epinephrine gland where cortisol is produced:

Thyrotrophic hormone (ТТH)

It is necessary for the normal functioning of thyroid gland:

24. Hormones of posterior pituitary (3 hormones)?

Hormone Released Chemical Class Target tissues/ organs Chief function of

Effect of T4 and T3 on Metabolism

Carbohydrate Protein Lipid

26. Hormones of pancreas (4 hormones)?

Insulin Activates a transport of

 Nature: protein (51 АA)

 Regulation of the synthesis:

It is destroyed by insulinase (enzyme of liver) to amino acids

28. Sex hormones: kinds, structure, place of synthesis?

Sex hormones released by Gonads

29. Hormones of adrenalcortex - corticosteroids. Two groups of corticosteroids?

Hormones of Adrenal cortex: