PMID: 6171809Oct 1, 1981Paper

Structure of the zeta chain of human embryonic hemoglobin

Proceedings of the National Academy of Sciences of the United States of America
J B Clegg, J Gagnon

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.

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Citations

Jan 1, 1982·Journal of Molecular Evolution·A H Reisner, N H Westwood
Jul 4, 2002·Molecular Aspects of Medicine·Thomas Brittain
Oct 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·S W ChungD H Chui
Oct 11, 1982·Nucleic Acids Research·P WinichagoonD J Weatherall
Aug 20, 2005·Proceedings of the National Academy of Sciences of the United States of America·Fan LuGrace Wahba
Nov 15, 1991·Journal of Chromatography·K Bhaumik
May 29, 2007·Experimental and Molecular Pathology·D Radford Shanklin
Jan 1, 1984·Pathology·D Todd

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