通过热变化的核磁共振自旋转移测定的一种酶的稳态参数。
Steady-state parameters of an enzyme from n.m.r. spin transfer with thermal variation.
作者信息
Kuchel P W
机构信息
Department of Biochemistry, University of Sydney, N.S.W., Australia.
出版信息
Biochem J. 1987 May 15;244(1):247-8. doi: 10.1042/bj2440247.
Abstract
N.m.r. spin-exchange analysis of enzymic reactions at chemical equilibrium is akin to radioactive-tracer-exchange analysis; unidirectional flux rates are obtained for the overall reaction. These data, by themselves, are not sufficient to define the values of all the individual rate constants or steady-state parameters. However, it is shown that, by measuring the dependence of the exchange rate constants on solute concentration and temperature, the individual rate constants, and hence the steady-state parameters, can be obtained for a simple enzyme system.
摘要
处于化学平衡状态的酶促反应的核磁共振自旋交换分析类似于放射性示踪剂交换分析；可获得整个反应的单向通量率。仅凭这些数据不足以确定所有单个速率常数或稳态参数的值。然而，研究表明，通过测量交换速率常数对溶质浓度和温度的依赖性，对于一个简单的酶系统，可以获得单个速率常数，进而得到稳态参数。
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