Haemoglobin
Hb isa conjugated protein
of metaloporphyrin.
It is the red pigment inside
the RBC.
Heam- 4% Globin- 96%
Molecular weight is 68000.
3.
Functions of Haemoglobin
•Transport oxygen from lung to tissues
• Transport CO2 to lungs
• Maintains acid base balance ( As a Buffer)
• Reserves Fe & Proteins
4.
Disadvantages if haemoglobinpresent in plasma.
Increase viscosity.
Increase osmotic pressure.
Rapid destruction by
reticuloendothelial system.
Haemoglobinuria
( excretion through kidney)
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
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.
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
9.
Attachment of Haemeto 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.
10.
Attachment of Haemeto Globin.
• Globin helps the Fe to
remain Fe++ form combine
O2 loosely.
• Carbonic anhydrase
remain only into RBC, help
CO2 transport as
bicarbonate form.
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