Abstract
Abstract Some of the equilibrium and kinetic constants for the reactions of the isolated γ chains of human fetal hemoglobin have been determined. As was previously found for the isolated β chain of human hemoglobin A, these constants are very different for the γ chain with its sulfhydryl group combined with p-mercuribenzoate as compared to those for the γ chain with a free sulfhydryl group. Since the human γ chain contains a single sulfhydryl group at position 93, the alteration in the heme reactivity can be attributed to the chemical modification of that residue.
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