堪萨斯血红蛋白分离亚基的氧平衡与动力学
Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas.
作者信息
Riggs A, Gibson Q H
出版信息
Proc Natl Acad Sci U S A. 1973 Jun;70(6):1718-20. doi: 10.1073/pnas.70.6.1718.
The isolated beta subunit of hemoglobin Kansas has an oxygen affinity that is as low relative to the oxygen affinity of the beta(A) subunit as the affinity of hemoglobin Kansas is low relative to hemoglobin A. Thus the low affinity properties of hemoglobin Kansas are almost completely reflected in the properties of the isolated subunits. The kinetic results show that the equilibrium affinity difference results both from a much larger oxygen dissocation rate constant in beta(Kansas) (k = 37 sec(-1) and 18 sec(-1) for beta(Kansas) and beta(A), respectively) and from a lower association reaction rate, The properties of the alpha chains from hemoglobins A and Kansas appear to be identical, as expected.
血红蛋白堪萨斯的分离β亚基具有的氧亲和力，相对于β（A）亚基的氧亲和力而言较低，就如同血红蛋白堪萨斯相对于血红蛋白A的亲和力较低一样。因此，血红蛋白堪萨斯的低亲和力特性几乎完全反映在分离亚基的特性中。动力学结果表明，平衡亲和力差异既源于β（堪萨斯）中氧解离速率常数大得多（β（堪萨斯）和β（A）的k分别为37秒⁻¹和18秒⁻¹），也源于缔合反应速率较低。正如预期的那样，血红蛋白A和堪萨斯的α链特性似乎是相同的。
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