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Fetal Hemoglobin and 2,3 BPG
The developing fetus expresses a slightly different hemoglobin molecule. The fetal hemoglobin consists of the same two identical alpha units as in adult hemoglobin but the two beta units are replaced by two identical gamma units. These gamma units differ in their sequence of amino acids and one important variation lies in the substitution of lysine 82 for serine. Lysine 82 carries a positive charge that allows the binding of 2,3-BPG to the center pocket of adult hemoglobin. Because this positive charged lysine is replaced with a neutral serine residue in fetal hemoglobin, the 2,3-BPG will not be able to bind as well to the center pocket. As a result, fetal hemoglobin will have a lower affinity for oxygen and the oxygen binding curve for fetal hemoglobin will shift towards the left side. Physiologically this is an important phenomenon because it allows the fetal hemoglobin to successfully transport the oxygen from the mother to the developing fetus.
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