Imai K, Yonetani H
Biochim Biophys Acta. 1977 Jan 25;490(1):164-70. doi: 10.1016/0005-2795(77)90116-7.
The effect of oxygen-linked tetramer-dimer dissociation on oxygen equilibrium of hemoglobin was investigated by measuring the equilibrium curves over a wide range of protein concentration. A Hill scheme which takes the subunit dissociation into account describes well the overall concentration dependences of the oxygen pressure and slope of the Hill plot at half saturation. Values of dissociation constant for oxyhemoglobin estimated from the equilibrium data agree with the vaues measured by other methods for phosphate-free and diphosphoglycerate-added hemoglobin. The present results indicate that oxygen equilibrium properties are only slightly influenced bysubunit dissociation in the concentration range above 60 muM (as heme) at which most equilibrium experiments have been carried out.
通过在很宽的蛋白质浓度范围内测量平衡曲线，研究了氧连接的四聚体-二聚体解离对血红蛋白氧平衡的影响。考虑亚基解离的希尔方程很好地描述了氧分压和半饱和时希尔图斜率的总体浓度依赖性。从平衡数据估算的氧合血红蛋白解离常数的值与通过其他方法测量的无磷酸盐和添加二磷酸甘油酸的血红蛋白的值一致。目前的结果表明，在大多数平衡实验所进行的高于60μM（以血红素计）的浓度范围内，亚基解离对氧平衡特性的影响很小。
