肌球蛋白亚片段-1 K+活化atp酶的动力学研究。

G S Kelemen, K Pintér
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引用次数: 0

摘要

测定了不同条件下肌球蛋白亚片段-1的K+活化atp酶活性,并计算了酶动力学参数。在低KCl浓度下,Km的对数随离子强度呈线性变化,另一方面,在低KCl浓度下,k2对离子强度的对数明显偏离线性。ADP是一种竞争性抑制剂,就像肌凝蛋白atp酶一样,并且实际上具有相同的抑制剂常数。S-1- ATP复合物分解(产物和酶)的能量参数与肌凝蛋白的能量参数特别相同,但其形成参数与肌凝蛋白的相应值不同:肌凝蛋白的δ SI相当大,δ HI明显更高。这可能是肌凝蛋白两个头相互作用的结果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A kinetic study of the K+ activated ATPase of myosin subfragment-1.

The K+ activated ATPase activity of myosin subfragment-1 was measured under different conditions and enzyme kinetic parameters were calculated. The logarithm of Km varies linearly with ionic strength down to very low KCl concentrations, the logarithm of k2 vs. ionic strength, on the other hand, considerably deviates from linearity at low concentrations of KCl. ADP is a competitive inhibitor, like myosin ATPase, and with practically the same inhibitor constant. The energetical parameters of the decomposition (to products and enzyme) of the S-1--ATP complex are partically the same as those for myosin, the parameters of its formation, however, differ from the corresponding values for myosin: delta SI is considerably, delta HI significantly higher in the case of myosin. This may be the result of some kind of interaction of the two heads of myosin.

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