This document discusses haemoglobin, including its composition, function, levels in adults and children, types, and synthesis. Some key points: - Haemoglobin is a conjugated protein made of heme (4%) and globin (96%) that transports oxygen and carbon dioxide in red blood cells. - It functions to transport oxygen from the lungs to tissues, carbon dioxide to the lungs, and helps maintain acid-base balance. - Normal haemoglobin levels vary based on age and sex, from 13.5-19.5 g/dL in cord blood to 8-10 g/dL in infants and 10-13 g/dL in children. - There are different types of haemoglobin

1. Haemoglobin
 Hb is a conjugated protein
of metaloporphyrin.
 It is the red pigment inside
the RBC.
 Heam- 4% Globin- 96%
 Molecular weight is 68000.
Dr. SAYID

2. Dr. SAYID

3. Functions of Haemoglobin
• Transport oxygen from lung to tissues
• Transport CO2 to lungs
• Maintains acid base balance ( As a Buffer)
• Reserves Fe & Proteins
Dr. SAYID

4. Disadvantages if haemoglobin
present in plasma.
Increase viscosity.
Increase osmotic pressure.
Rapid destruction by
reticuloendothelial system.
Haemoglobinuria
( excretion through kidney)
Dr. SAYID

5. Adult Male
• 13 – 18 g/dl
Adult Female
• 11.5 - 16.5 g/dl
Full term baby (Cord blood)
• 13.5 – 19.5 g/dl
Infant (1 year)
8 – 10 g/dl
Child
10 - 13 g/dl
Dr. SAYID
Normal Hb
Level

6.  Testosterone stimulate
Erythropoisis, for that Hb
level is higher than female.
1st day at birth Hb level is
high, then reduce from 3rd
month to 1 year. Then Hb
raise slowly through
childhood to adult. Dr. SAYID

7. Grading of anemia
Mild Upto 11 g/dl
Moderate 11- 9 g/dl
Severe < 9 g/dl
Dr. SAYID

8. Synthesis of Hemoglobin
 2 succinyl – CoA + 2 glysine Pyrrole
 4 Pyrrole Protoporphyrin IX
 Protoporphyrin IX + Fe2+ Heme
 Globin 4 polypeptide chains ( 2 Alpha+ 2 Beta)
 Heme + Globin Hemoglobin
Dr. SAYID

9. Attachment of Haeme to Globin.
• 4 units of Haem attached
to 1 unit of Globin.
• So 1 Haemoglobin
molecules contains 4 Iron
Atoms which carry 4
molecules of oxygen.
Dr. SAYID

10. Attachment of Haeme to Globin.
• Globin helps the Fe to
remain Fe++ form combine
O2 loosely.
• Carbonic anhydrase
remain only into RBC, help
CO2 transport as
bicarbonate form.
Dr. SAYID

11. Hb A - 2α+2β
HbA2 - 2α+2δ
Hb-F – 2α+2γ
Hb Bart’s
Hb Gower - 1
Hb-Gower -2
Hb Portland
Types of Hb
Adult
Fetal
Embryonic
Normal
Dr. SAYID

12. Types of Hb
Hb - S
Hb - C
Hb – D Panjub Abormal
Hb - E
Dr. SAYID

13. Hb A - 2α+2β 98%
HbA2 - 2α+2δ 2%
Hb-F - 2α+2γ 0-1 %
Sickle Cell Haemoglobin
Hb-M
Hb C
Physiological Pathological
Dr. SAYID

14. FETAL HAEMOGLOBIN
• Normally present in fetal RBC (70% Hb-F &
30% Hb-A)
• Disappear in 2-3 months after birth.
• Structure
– 4 polypeptide chains (2 α + 2 γ)
• Characteristics.
– Affinity for oxygen –more
– Carry 20-30% more O2 than Hb-A
– Resistance to action of alkalies
– Life span – less.
Dr. SAYID