Structure of the zeta chain of human embryonic hemoglobin.

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Abstract
The complete amino acid sequence of the .zeta. chain of human embryonic Hb was been determined. It differs from human .alpha. globin at 57 of the 141 residues and several of the replacements are at positions of structural or functional importance, particularly in relationship to the Bohr effect and high intrinsic O2 affinity which are characteristic of embryonic Hb. The .zeta.-globin sequence is more closely related to other mammalian embryonic .alpha.-like globins than to human .alpha., suggesting that there have been strong selective pressures to maintain these embryo-specific globins since their emergence several hundred millions years ago.