氧与三种人类胚胎血红蛋白结合的变构调节。
Allosteric modulation of oxygen binding to the three human embryonic haemoglobins.
作者信息
Hofmann O, Mould R, Brittain T
机构信息
Biochemistry and Molecular Biology Research Group, School of Biological Sciences, University of Auckland, New Zealand.
出版信息
Biochem J. 1995 Mar 1;306 ( Pt 2)(Pt 2):367-70. doi: 10.1042/bj3060367.
Abstract
Plasmid based yeast expression systems have been developed for the high-level expression of the three human embryonic haemoglobins Gower I (zeta 2 epsilon 2), Gower II (alpha 2 epsilon 2) and Portland (zeta 2 gamma 2). Physiochemical characterization of the three product haemoglobins show them to be in the 'native' state. Oxygen-binding studies show that, under what are usually considered physiological conditions, each of the embryonic haemoglobins shows a high oxygen affinity, coupled to a high degree of co-operativity. Allosteric modulation of the oxygen-binding properties of the three haemoglobins in response to organic phosphates and protons has been investigated. The various responses exhibited by the three haemoglobins are rationalized in terms of their amino acid sequences.
摘要
基于质粒的酵母表达系统已被开发用于高效表达三种人类胚胎血红蛋白，即戈尔I（ζ2ε2）、戈尔II（α2ε2）和波特兰（ζ2γ2）。对这三种产物血红蛋白的物理化学特性分析表明它们处于“天然”状态。氧结合研究表明，在通常被认为是生理条件下，每种胚胎血红蛋白都表现出高氧亲和力，并伴有高度协同性。已经研究了这三种血红蛋白对有机磷酸盐和质子的氧结合特性的变构调节。根据它们的氨基酸序列，对这三种血红蛋白表现出的各种反应进行了合理的解释。
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