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A. BLOOD CHEMISTRY
OUTLINE
I. I. Blood Total Circulating Blood Volume: 5-6 liters (6-8% of total
A. Blood Chemistry body weight)
B. Blood Composition Color:
C. Function of Blood → Arterial oxygenated blood: crimson/bright red
D. Plasma and Serum → Venous deoxygenated blood: dark red, purplish
II. Red Blood Cell pH: 7.35-7.45 (Ave. 7.40)
A. Structure and Characteristics Specific Gravity: 1.035-1.075
B. RBC Membrane Proteins Average blood volumes
C. Membrane Transporters Premature Neonates 95 mL/kg
D. Formation of Erythrocytes Full Term Neonates 85 mL/kg
III. RBC Metabolism of Glucose
Infants 80 mL/kg
A. Embden-Meyerhoff Pathway
B. Hexose Monophosphate Pathway
Adult Men 75 mL/kg
C. Rapaport-Luebering Shunt Adult Women 65 mL/kg
D. Gluthatione System
IV. Hemoglobin Synthesis B. BLOOD COMPOSITION
A. Hemoglobin
B. Porphyrin ● Formed Elements (40-45% of Blood Composition)
C. Heme → Red Blood Cells (Erythrocytes) - most abundant; delivers
V. Degradation of Hemoglobin oxygen
A. Synthesis of Unconjugated Bilirubin → Buffy Coat (<1%)
B. Metabolism of Bilirubin in the Liver ▪ White Blood Cells (Leukocytes) - fights infection
C. Fate in the Intestines ▪ Platelets (Thrombocytes) - stops bleeding; controls
D. Unconjugated Vs. Conjugated Bilirubin hemostasis (blood clotting)
E. Hyperbilirubinemia ● Plasma (55% of Blood Composition)
F. Jaundice
VI. Porphyrias
A. Types of Porphyrias
B. ALA Synthesis
VII. RBC Disorders
A. Enzyme Deficiencies
B. Hemoglobinopathies
VIII. Review Questions
IX. References
OBJECTIVES
1. Given a patient with abdominal pain and dark urine, Figure 1. Composition of Blood Components.
identify the biochemical pathways or processes that are
involved. Hematocrit: Blood volume % occupied by Red blood cells
2. Apply the biochemical concepts and principles that will
help explain the development of porphyrias
Males: 40-45% Females: 38-42%
3. Correlate the biochemical or molecular basis with the Used in diagnosis of anemias and polycythemia
clinical manifestation of the disease, the findings on
physical examination of the patient and laboratory C. FUNCTION OF BLOOD
results.
4. Discuss the biochemical basis of the management of ● Transport
porphyrias → Oxygen: lungs to tissue
→ CO2: tissue to lungs
→ Absorbed nutrients (e.g. fats, proteins): intestines to
I. BLOOD areas of utilization
→ Hormones: organs of synthesis to distant sites
Fluid connective tissue derived from the mesoderm of the → Metabolites and waste products (e.g. urea) for excretion
germ layer, which consists of plasma and formed elements ● Homeostasis
(RBC, WBC, and platelets). acid- base balance
Formed elements are produced in the red bone marrow water balance between tissues and circulation
The proteins in plasma are produced by liver, the enzymes adequate blood supply and hemostasis
and antibodies are produced by cellular component of ● Regulation (Temperature and Metabolism)
blood ● Defense mechanism of the body (WBCs and circulating
Circulates in the body via the blood vessels and heart antibodies)
Trans # 5 Group 26: De Torres, Deato, Dee, Del Rosario Trans Head: Canete 1 of 11
D. PLASMA AND SERUM ● Lifespan: 90-120 days
● Compounds found in RBC
Table 1. Comparison of Plasma and Serum hemoglobin (iron-binding protein)
NADH-cytochrome b5 methemoglobin reductase,
Plasma Serum Nitric Oxide
Glycolytic enzymes
Whole blood without formed GSH (reduced glutathione)
Whole blood without elements and clotting factors (I or
formed elements B. RBC MEMBRANE PROTEINS
fibrinogen, II, V, VIII)
● Integral proteins: span the whole length of lipid bilayer
Centrifuged with → Band 3: also known as AE1 (anion exchanger 1); most
Centrifuged coagulated blood
anticoagulant abundant protein in RBC membrane; plays a role in
chloride bicarbonate exchange
Used in reference to → Glycophorin: single pass membrane; heavily
Used in reference to laboratory glycosylated; gives RBC hydrophilic charged coat (for
physiologic or pathological
values repulsion to cells and vessel walls)
processes
● Peripheral proteins: found inside cell, on the cytoplasmic
surface of lipid bilayer; for membrane stability and elasticity.
Blood transfusion, Blood typing, diagnosis, antibody → Spectrin: most abundant protein of RBC; major protein
diagnosis culture of the cytoskeleton of RBC; encompasses whole top part
of membrane; confers flexibility
→ Actin: band 5
● Plasma - non-cellular, fluid component of blood; cloudy, → Ankyrin: binds spectrin; binds tightly to band 3, securing
pale or grayish yellow liquid attachment of spectrin to membrane
→ Band 4.1: globular protein; binds to end of spectrin; may
→ Composed of water and dissolved solutes
interact with membrane phospholipids, connecting lipid
● Serum - blood plasma without clotting factors; clear bilayer to cytoskeleton.
yellowish liquid
Reticulocyte Count
Immature red blood cells occurs in the circulation
approximately 1%
Increased reticulocyte count indicates premature
+ blood loss during haemolytic anemia
C. Rapaport-Luebering Shunt
4 polypeptide Single
Figure 8. Glutathione System chains: 2α + 2β polypeptide
Structure
chain
Free Radicals Tetramer
Free radicals are atoms, ions, or molecules that
Increases
contain an unpaired electron. The unpaired electron High affinity
makes them unstable and highly reactive. Affinity for O2 proportionally
even in low [O2]
with [O2]
Includes Reactive Oxygen Species (ROS)
Number of heme
groups/binding 4 1
sites
Figure 9. Porphyrin Structure. Rings labeled as I, II, III, Iv. Methyne Briges
as α β γ δ. Subsituent positions as 1 - 8 Figure 11. Structure of Heme
● Around 200 billion Red Blood Cells are degraded in the adult A. SYNTHESIS OF UNCONJUGATED BILIRUBIN
human body daily
● The Globin component is degraded and incorporated into the ● This occurs in the reticuloendothelial cells present in the liver,
amino acid pool spleen, and bone marrow.
● The heme is catabolized into bilirubin, a yellowish pigment in ● The iron of the heme group is oxidized in its ferric (Fe3+) form.
the bile. ● The enzyme, Heme oxygenase, converts heme into biliverdin
through the consumption of 3 moles of O2 and 7 electrons,
Transport Proteins and their ligands which are donated by NADH and NADPH-cytochrome P450
reductase.
Table 6. Proteins and Ligands pointed out by Dr. Reyes ● This reaction releases Carbon Monoxide and the Iron, which is
transported using transferrin into the iron pool.
Proteins Ligands ● The methylene bridges found in the center are reduced into
3+ methyl groups using another enzyme, Biliverdin reductase.
Transferrin Fe
This produces unconjugated Bilirubin which is nonpolar or
not water-soluble.
Hemoglobin/protoporphyrin- Heme, bilirubin, bilverdin
● This Unconjugated Bilirubin is bound to albumin and is
binding albumin
transported into the liver.
Haptoglobin Hemoglobin dimers
● Unconjugated Bilirubin:
→ Indirect reacting to Erlich’s diazo reagent test
Figure 14. Synthesis and Structure of Unconjugated Bilirubin → “Indirect bilirubin”
→ Hydrophobic and can cross the blood brain barrier
B.METABOLISM OF BILIRUBIN IN THE LIVER → Free Bilirubin
● Conjugated Bilirubin:
→ Direct reacting to Erlich’s diazo reagent test
→ “Direct Bilirubin”
→ Hydrophilic and can be excreted from the body
● Importance of Conjugated Bilirubin: It is water – soluble, thus it
can be excreted from the body.
E. HYPERBILIRUBINEMIA
F. JAUNDICE
● “Icterus”
● Bilirubin is 2- 2.5 mg/dl in the blood.
● Appears yellowish because the bilirubin diffuses into the tissues
Decreased NADPH
↓
Decreased amount of reduced glutathione
↓
Increased conversion of hemoglobin to methemoglobin
↓
Decreased RBC lifespan
↓
HEMOLYTIC ANEMIA
Answers: b, d, c, c, c, d, a, e, c, b
IX. REFERENCES
Dr Reyes’ Powerpoint
Transes of 2020A, 2020C
Harper’s Illustrated Biochemistry, 30th Ed.
Mark’s Basic Medical Biochemistry, 4th Ed.