血红蛋白协同氧结合机制（自旋标记三磷酸协同转变模型-切萨皮克血红蛋白）
Mechanism of cooperative oxygen binding to hemoglobin (spin-labeled triphosphate-concerted transition model-hemoglobin chesapeake).
作者信息
Ogata R T, McConnell H M
出版信息
Proc Natl Acad Sci U S A. 1972 Feb;69(2):335-9. doi: 10.1073/pnas.69.2.335.
Abstract
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 alpha(2) (+CN)beta(2) and alpha(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 alpha-subunits are treated as nonequivalent to the beta-subunits.
摘要
有证据表明，广义协同转变模型能够定量理解：（a）部分配体化血红蛋白溶液中存在的分子种类，以及（b）协同性的大分子机制。通过研究自旋标记三磷酸酯与无配体和部分配体化血红蛋白溶液以及杂种α(2)(+CN)β(2)和α(2)β(2)(+CN)的结合，确定了血红蛋白A和血红蛋白切萨皮克的模型参数。该模型与最初由莫诺德、怀曼和尚热[《分子生物学杂志》（1965年）12卷，88页]提出的血红蛋白模型相同，只是α亚基被视为与β亚基不等价。
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