人血红蛋白中氧合作用与亚基解离之间的联系。
The linkage between oxygenation and subunit dissociation in human hemoglobin.
作者信息
Ackers G K, Halvorson H R
出版信息
Proc Natl Acad Sci U S A. 1974 Nov;71(11):4312-6. doi: 10.1073/pnas.71.11.4312.
Abstract
The use of subunit dissociation as a means of probing intersubunit contact energy changes which accompany cooperative ligand binding has been studied for the case of human hemoglobin. An analysis is presented delineating the information that can be obtained from the linkage relationships between ligand binding and subunit dissociation of hemoglobin tetramers into dimers. The analysis defines (a) the variation of the saturation function, Y, with total protein concentration, (b) the variation of the subunit dissociation constant (x)K(2) with ligand concentration (X) and (c) the correlations between changes in dimer-dimer contact energy and the sequential ligand binding steps. Sensitivity of the linkage function has been explored by numerical simulation. It is shown that subunit dissociation may appreciably affect oxygenation curves under usual conditions of measurement and that relying solely on either (x)K(2) or Y may lead to incorrect picutres of the energetics, whereas the combination defines the system much more exactly.
摘要
对于人血红蛋白的情况，已经研究了使用亚基解离作为探测伴随协同配体结合的亚基间接触能变化的一种手段。本文给出了一种分析方法，阐述了从血红蛋白四聚体解离为二聚体的配体结合与亚基解离之间的连锁关系中可以获得的信息。该分析定义了：(a) 饱和函数Y随总蛋白浓度的变化；(b) 亚基解离常数(x)K(2)随配体浓度(X)的变化；以及(c) 二聚体 - 二聚体接触能变化与顺序配体结合步骤之间的相关性。通过数值模拟探索了连锁函数的敏感性。结果表明，在通常的测量条件下亚基解离可能会显著影响氧合曲线，仅依靠(x)K(2)或Y可能会导致对能量学的错误描述，而将两者结合能更准确地定义该系统。
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