文章基本信息

标题：Structure of the zeta chain of human embryonic hemoglobin
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作者：J B Clegg ; J Gagnon
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：10
页码：6076-6080
DOI：10.1073/pnas.78.10.6076
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.