文章基本信息

标题：Mechanism of Cooperative Oxygen Binding to Hemoglobin
本地全文：下载
作者：Ronald T. Ogata ; Harden M. McConnell
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：1972
卷号：69
期号：2
页码：335-339
DOI：10.1073/pnas.69.2.335
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Evidence is presented that a generalized concerted transition model provides a quantitative understanding of (a) the molecular species that are present in solutions of partially liganded hemoglobin and (b) the macromolecular mechanism of cooperativity. Model parameters for hemoglobin A and for hemoglobin Chesapeake were determined from studies of the binding of spin-label triphosphates to ligand-free and partially liganded hemoglobin solutions, and to the hybrids [α]2+CN{beta}2 and [α]2{beta}2+CN. This model is the same as that proposed originally by Monod, Wyman, and Changeux [J. Mol. Biol. (1965) 12, 88] for hemoglobin, except that the [α]-subunits are treated as nonequivalent to the {beta}-subunits.
关键词：spin-labeled triphosphate ; concerted transition model ; hemoglobin Chesapeake