Haemoglobin

Haemoglobin (Hb) lecture by Dr. Sayid
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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. Dr. SAYID Normal Hb Level

6. Testosterone stimulate Erythropoisis, for that Hb level is higher than female. 1 st day at birth Hb level is high, then reduce from 3 rd 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. 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. 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