α链和β链对血红蛋白结合氧和解离氧动力学的贡献。
The contribution of the alpha and beta chains to the kinetics of oxygen binding to and dissociation from hemoglobin.
作者信息
Gibson Q H
出版信息
Proc Natl Acad Sci U S A. 1973 Jan;70(1):1-4. doi: 10.1073/pnas.70.1.1.
Abstract
A new type of experiment in which hemoglobin is exposed briefly to oxygen has shown that the half-time of dissociation of oxygen from some partly oxygenated intermediates is about 1 msec at 20 degrees and 10 msec at 2 degrees . The rapid dissociation occurs selectively from one type of chain, provisionally identified as the beta-chain. Chains that show the rapid rate of dissociation of oxygen also bind rapidly. It follows that the kinetic equivalent of the Adair equation and the Monod-Wyman-Changeux model are quite unsuited to represent the kinetics of the oxygen-hemoglobin reaction. The reaction of oxygen with hemoglobin closely resembles that of the alkyl isocyanides and differs radically from that of carbon monoxide.
摘要
一种新型实验表明，血红蛋白短暂暴露于氧气中时，在20摄氏度下，一些部分氧化中间体的氧解离半衰期约为1毫秒，在2摄氏度下为10毫秒。快速解离选择性地发生在一种暂时被确定为β链的链上。显示出快速氧解离速率的链也能快速结合。由此可见，阿代尔方程和莫诺-怀曼-尚热模型的动力学等效式完全不适用于描述氧合血红蛋白反应的动力学。氧与血红蛋白的反应与烷基异氰化物的反应非常相似，与一氧化碳的反应则有根本区别。
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