2,3-二磷酸甘油酸与各种人类血红蛋白的相互作用。
The interaction of 2,3-diphosphoglycerate with various human hemoglobins.
作者信息
Bunn H F, Briehl R W
出版信息
J Clin Invest. 1970 Jun;49(6):1088-95. doi: 10.1172/JCI106324.
Abstract
Oxygen equilibria were measured on a number of human hemoglobins, which had been "stripped" of organic phosphates and isolated by column chromatography. In the presence of 2 x 10(-4) M 2,3-diphosphoglycerate (2,3-DPG), the P(50) of hemoglobins A, A(2), S, and C increased about twofold, signifying a substantial and equal decrease in oxygen affinity. Furthermore, hemoglobins Chesapeake and M(Milwaukee-1) which have intrinsically high and low oxygen affinities, respectively, also showed a twofold increase in P(50) in the presence of 2 x 10(-4) M 2,3-DPG. In comparison to these, hemoglobins A(IC) and F were less reactive with 2,3-DPG while hemoglobin F(I) showed virtually no reactivity. The N-terminal amino of each beta-chain of hemoglobin A(IC) is linked to a hexose. In hemoglobin F(I) the N-terminal amino of each gamma-chain is acetylated. These results suggest that the N-terminal amino groups of the non-alpha-chains are involved in the binding of 2,3-DPG to hemoglobin.
摘要
对多种已通过柱色谱法“去除”有机磷酸盐并分离出来的人血红蛋白进行了氧平衡测定。在存在2×10⁻⁴ M 2,3 -二磷酸甘油酸（2,3 - DPG）的情况下，血红蛋白A、A₂、S和C的P₅₀增加了约两倍，这表明氧亲和力大幅且同等程度地降低。此外，分别具有固有高氧亲和力和低氧亲和力的切萨皮克血红蛋白和M（密尔沃基 - 1）血红蛋白，在存在2×10⁻⁴ M 2,3 - DPG时，P₅₀也增加了两倍。与之相比，血红蛋白A(IC)和F与2,3 - DPG的反应性较低，而血红蛋白F(I)几乎没有反应性。血红蛋白A(IC)每条β链的N端氨基与一个己糖相连。在血红蛋白F(I)中，每条γ链的N端氨基被乙酰化。这些结果表明，非α链的N端氨基参与了2,3 - DPG与血红蛋白的结合。
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