STRUCTURE OF HAEMOGLOBIN

STRUCTURE OF HAEMOGLOBIN IS DESCRIBED HERE BRIEFLY

1. Structure of haemoglobin Presented by: A yesha Kabeer UNIVERSITY OF GUJRAT SIALKOT SUB CAMPUS

2. HAEMOGLOBIN Red colored  conjugated protein  (made up of H aem and Globin) present inside the RBC Normal Hb% in adult male is  14 to 16 gm. Approximately  6.25 gm of Hb are synthesized  and destroyed every day. Haem structure does not vary from species to species. It is the basic protein globin that varies in amino acid composition and sequence in different species. Globin is rich in Histidine and Lysine .

3. STRUCTURE OF HAEMOGLOBIN

4. STRUCTURE OF HAEMOGLOBIN : Haem : Haem is iron  porphyrin compound.  Porphyrin is a  tetrapyrrole structure . Ferrous iron occupies the center of the porphyrin ring and establishes linkages with all the four nitrogens of all the pyrrole rings. It is also linked to nitrogen of imidazole ring of histidine present in globin part.

5. Haem structure:

6. 2. Globin : Globin part is made of four polypeptide chains, to identical α-chains and two identical β-chains in normal adult haemoglobin . Each chain contains a “ haem” in the so called ‘ haem pocket’. So one Hb molecule possess four haem units. Hb molecule contains hydrophobic amino acids inside and hydrophilic ones on the surface.