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In fetal hemoglobin (HbF), the two β subunits are replaced with two γ subunits. The result...

In fetal hemoglobin (HbF), the two β subunits are replaced with two γ subunits. The result is that HbF has a higher affinity for oxygen than the mother’s adult hemoglobin (HbA). The greater oxygen affinity of HbF compared with HbA is due to:

a) the γ and β subunits of HbF exhibit a greater degree of cooperativity than the α and β subunits of HbA.

b) the decreased affinity of the γ subunits for CO2.

c) the decreased affinity of 2,3‑BPG to the γ subunits of HbF.

d) a different mode of binding between the heme ring and the γ globin peptide.

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Answer #1

Correct answer is c) the decreased affinity of 2,3‑BPG to the γ subunits of HbF.

Because structural difference in both affects the BPG binding leading to differential function of both.

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