人类胚胎血红蛋白ζ链的结构
Structure of the zeta chain of human embryonic hemoglobin.
作者信息
Clegg J B, Gagnon J
出版信息
Proc Natl Acad Sci U S A. 1981 Oct;78(10):6076-80. doi: 10.1073/pnas.78.10.6076.
Abstract
The complete amino acid sequence of the zeta chain of human embryonic hemoglobin has 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 oxygen affinity which are characteristic of embryonic hemoglobins. 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 million years ago.
摘要
人类胚胎血红蛋白ζ链的完整氨基酸序列已被确定。它在141个残基中有57个与人类α珠蛋白不同，其中一些替换发生在具有结构或功能重要性的位置，特别是与胚胎血红蛋白特有的玻尔效应和高固有氧亲和力相关的位置。ζ珠蛋白序列与其他哺乳动物胚胎α样珠蛋白的关系比与人类α珠蛋白的关系更密切，这表明自数亿年前这些胚胎特异性珠蛋白出现以来，一直存在强大的选择压力来维持它们。
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