pH dependence of 2,3-diphosphoglycerate binding to human hemoglobin A0 at 21.5 degrees C.
pH dependence of 2,3-diphosphoglycerate binding to human hemoglobin A0 at 21.5 degrees C.
复制标题
21.5 摄氏度下 2,3-二磷酸甘油酸与人血红蛋白 A0 结合的 pH 依赖性。
DOI：
10.1002/prot.340010208
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发表时间：
1986
期刊：
影响因子：
2.9
通讯作者：
Powers,DA
中科院分区：
文献类型：
--
作者：
Hobish,MK;Powers,DA
使用速率平衡透析来测量 2,3-二磷酸甘油酸 (DPG) 在 pH 5-9 范围内、21.5°C 下与人氧合血红蛋白和脱氧血红蛋白 AO 的结合。这种方法产生了一组准确、精确且自洽的独立于模型的关联常数。这些数据已成功拟合到功能类似于希尔方程的热力学模型。通过该拟合过程生成的等温线似乎在低 pH 值下相交并在高 pH 值下收敛。高 pH 值下的这种明显收敛与在 DPG 饱和条件下进行的氧平衡研究获得的结果一致。这些计算出的等温线用于确定玻尔效应随 pH 值的变化的增强情况。这些结果与其他研究人员通过 pH 统计测量获得的数据一致。本文介绍了一系列研究中的第一篇，这些研究将系统地描述血红蛋白和 DPG 之间的相互作用。
Rate equilibrium dialysis was used to measure the binding of 2,3‐diphosphoglycerate (DPG) to human oxy‐ and deoxyhemoglobin AOover the range pH 5–9, at 21.5°C. This approach yielded an accurate, precise, and self‐consistent set of model‐independent association constants. These data were successfully fitted to a thermodynamic model which is fuctionally similar to a Hill equation. The isotherms generated by this fitting procedure appear to intersect at low pH and converge at high pH. This apparent convergence at high pH is consistent with results obtained by oxygen equilibria studies performed under conditions of saturating DPG. These calculated isotherms were used to determine the enhancement of the Bohr effect as a function of pH. These results are consistent with data obtained by pH stat measurements by other investigators.This paper presents the first in a series of studies that will provide a systematic characterization of the interaction between hemoglobin and DPG.