HEMOGLOBIN:
NORMAL RANGE
Male; 13.5-17.5 g/dl
Female; 12-15.5 g/dl
Foetus; 16-18 g/dl
New born;20-24 g/dl
Structure:
Hemoglobin, also spelled haemoglobin , iron containing protein in the
blood of many animals , in the red blood cells (erythrocytes)
of vertebrates that transports oxygen to the tissues.
Hemoglobin (mol.wt.64,450) is a conjugated protein ,containing globin-
the apoprotein part and the heme the non protein part(prosthetic
group).
Structure of globin; consists of four polypeptide chains of two different
primary structures.Two alpha chains and two beta chains.Each alpha
chain consists of 141 aminoacids and beta chain consists of 146
aminoacids.Each subunit contains a heme group.
Structure of heme; the characteristic red colour of hemoglobin is due to
heme.Heme contains a porphyrin molecule namely protoporphyrin
IX,with iron at its center. protoporphyrin IX consists of four pyrrole rings
to which four methyl, two propionyl and two vinyl groups are attached.
The iron ion, which is the site of oxygen binding, attached to six
coordinate bond :
Four coordinate bond to the four nitrogen atoms in the center of the
porphyrin ring, which all lie in one plane.
One coordinate bond to the globin chain via the N atoms of
the imidazole ring of F8 histidine residue below the porphyrin ring.
A sixth position can reversibly bind oxygen by a coordinate covalent
bond, completing the octahedral group of six ligands. This reversible
, bonding with oxygen is why hemoglobin is so useful for transporting
oxygen around the body.
Even though carbon dioxide is carried by hemoglobin, it does not
compete with oxygen for the iron-binding positions but is bound to
the amine groups of the protein chains attached to the heme groups.
Types:
Hemoglobin variants are a part of the
normal embryonic and fetal development.
In the embryo:
NORMAL RANGE
Male; 13.5-17.5 g/dl
Female; 12-15.5 g/dl
Foetus; 16-18 g/dl
New born;20-24 g/dl
Structure:
Hemoglobin, also spelled haemoglobin , iron containing protein in the
blood of many animals , in the red blood cells (erythrocytes)
of vertebrates that transports oxygen to the tissues.
Hemoglobin (mol.wt.64,450) is a conjugated protein ,containing globin-
the apoprotein part and the heme the non protein part(prosthetic
group).
Structure of globin; consists of four polypeptide chains of two different
primary structures.Two alpha chains and two beta chains.Each alpha
chain consists of 141 aminoacids and beta chain consists of 146
aminoacids.Each subunit contains a heme group.
Structure of heme; the characteristic red colour of hemoglobin is due to
heme.Heme contains a porphyrin molecule namely protoporphyrin
IX,with iron at its center. protoporphyrin IX consists of four pyrrole rings
to which four methyl, two propionyl and two vinyl groups are attached.
The iron ion, which is the site of oxygen binding, attached to six
coordinate bond :
Four coordinate bond to the four nitrogen atoms in the center of the
porphyrin ring, which all lie in one plane.
One coordinate bond to the globin chain via the N atoms of
the imidazole ring of F8 histidine residue below the porphyrin ring.
A sixth position can reversibly bind oxygen by a coordinate covalent
bond, completing the octahedral group of six ligands. This reversible
, bonding with oxygen is why hemoglobin is so useful for transporting
oxygen around the body.
Even though carbon dioxide is carried by hemoglobin, it does not
compete with oxygen for the iron-binding positions but is bound to
the amine groups of the protein chains attached to the heme groups.
Types:
Hemoglobin variants are a part of the
normal embryonic and fetal development.
In the embryo:
