HEMOGLOBIN

APPEARANCE AND SYNTHESIS

HUZAIFA IMDAD BHATTI

ROLL NO. 216
HEMOGLOBIN
 Red coloured
 Globular protein
 4 polypeptide chains (2 and 2
chains)
 Quaternary structure
 Contains iron
 Responsible for O2 transport
COMPOSITION
Heme part (containing Iron)

Globin chains
When does it appear during erythropoiesis?

 It appears during Polychromatophil Erythroblastic

stage of erythropoiesis.
 Large amount of hemoglobin appears in cytoplasm
during this stage.
SYNTHESIS OF HEMOGLOBIN
Synthesis of hemoglobin begins in Proerythroblast
(Pronormoblast ► first cells identified as
belonging of RBC series).
It continues till Reticulocyte stage of red blood
cells synthesis.
 STEPS OF SYNTHESIS
 FIRST STEP:
 Succinyl CoA (formed in Kreb’s cycle) binds with Glycine to form a pyrrole molecule.
 SECOND STEP:
 Four pyrrole molecules combine to form Protoporphyrin IX.
 THIRD STEP:
 Protoporphyrin IX combines with iron to form heme molecule.
 Heme formation takes place in Mitochondria.
 FOURTH STEP:
 Heme molecule combines with globin (polypeptide chain) to form hemoglobin chain.
 Globin chain formation takes place in Ribosomes.
FORMATION OF HEMOGLOBIN
CONFIGURATION
Hemoglobin contains four Polypeptide chains.
Each chain weighs 16,000 D.
Four of these chains combine to form hemoglobin
(Hb A) having weight of 64,458 D.
CHARACTERISTICS
Molecular Weight = 64,440 D
In RBC
34% wet weight
95% dry weight
 Intracellular Buffer
 Binds 4 oxygen molecules (8 oxygen atoms)
 1 g of Hb carries 1.34 ml of O2
ANY
QUESTIONS?