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Question

Hb-F has a higher affinity for O2 because

A
It binds BPG less strongly
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B
Its oxygen haemoglobi dissociation curve appears on the left side
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C
Hb-F can carry up to 30% more O2 than maternal Hb-A
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D
It having gamma polypetide chain
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Solution

The correct options are
A It binds BPG less strongly
B Its oxygen haemoglobi dissociation curve appears on the left side
D It having gamma polypetide chain
Hb is the hemoglobin pigment that is present in the red blood cells of blood that gives the blood red color. Hb-F is a type of hemoglobin which is present in the feotus of humans. They are composed of two gamma polypeptide chains, it is tetrameric structure. Thya has a higher affinity for the oxygen and thus shows the left curve, they do not bind or weakly bind to the BPG (Biphosphoglyceric acid) as it decreases the affinity of Hb to bind with oxygen. Hb-F bins to lesser oxygen molecules as reaches the saturated point much earlier than adult hemoglobin (Hb A).
So, the correct option is 'It binds BPG less strongly, Its oxygen-hemoglobin dissociation curve appears on the left side, and It's having gamma polypeptide chain'.


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