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Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data.

作者信息

Strickland S, Palmer G, Massey V

出版信息

J Biol Chem. 1975 Jun 10;250(11):4048-52.

PMID:1126943
Abstract
摘要

相似文献

1
Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data.根据快速反应动力学数据测定酶-底物(或蛋白质-配体)相互作用的解离常数和比速率常数。
J Biol Chem. 1975 Jun 10;250(11):4048-52.
2
Mechanism of malic enzyme from pigeon liver. Magnetic resonance and kinetic studies of the role of Mn2+.鸽肝苹果酸酶的作用机制。锰离子作用的磁共振及动力学研究。
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The determination of thermodynamic allosteric parameters of an enzyme undergoing steady-state turnover.处于稳态周转的酶的热力学别构参数的测定。
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An accurate method for determination of receptor-ligand and enzyme-inhibitor dissociation constants from displacement curves.一种从置换曲线测定受体-配体和酶-抑制剂解离常数的准确方法。
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Intermolecular ligand substitution reactions.分子间配体取代反应。
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Biochem J. 1973 Jun;133(2):255-61. doi: 10.1042/bj1330255.
7
[Kinetic behavior of slowly equilibrating association-dissociation enzyme systems].[缓慢平衡的缔合-解离酶系统的动力学行为]
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Exponential model for a two-ligand, regulatory enzyme. Part 1: computer programs for the determination of the model constants from initial velocity data.双配体调节酶的指数模型。第1部分:根据初始速度数据确定模型常数的计算机程序。
Int J Biomed Comput. 1981 Jul;12(4):291-313. doi: 10.1016/0020-7101(81)90042-8.
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