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Steady-state parameters of an enzyme from n.m.r. spin transfer with thermal variation.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。
Biochem J. 1987 May 15;244(1):247-8. doi: 10.1042/bj2440247.
2
PH-dependence of the steady-state rate of a two-step enzymic reaction.两步酶促反应稳态速率的pH依赖性
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Spin-exchange NMR spectroscopy in studies of the kinetics of enzymes and membrane transport.自旋交换核磁共振光谱法在酶动力学和膜转运研究中的应用
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The steady-state kinetics of isotope exchange for one substrate-one product enzymic reactions.单底物-单产物酶促反应的同位素交换稳态动力学。
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Rate limitation within a single enzyme is directly related to enzyme intermediate levels.单一酶内的速率限制与酶中间产物水平直接相关。
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One-substrate-one product enzymic reactions: the relationship between isotope-exchange kinetic, steady-state kinetic and equilibrium parameters.
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Isomerization of the free enzyme versus induced fit: effects of steps involving induced fit that bypass enzyme isomerization on flux ratios and countertransport.游离酶的异构化与诱导契合：涉及绕过酶异构化的诱导契合步骤对通量比和逆向转运的影响。
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Anomeric preference of fluoroglucose exchange across human red-cell membranes. 19F-n.m.r. studies.氟代葡萄糖跨人红细胞膜交换的异头偏好性。19F核磁共振研究。
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本文引用的文献

1
Uses and limitations of measurements of rates of isotopic exchange and incorporation in catalyzed reactions.催化反应中同位素交换和掺入速率测量的用途及局限性。
Arch Biochem Biophys. 1959 Jun;82(2):387-410. doi: 10.1016/0003-9861(59)90136-5.
2
A thermal-variation method for analysing the rate constants of the Michaelis--Menten mechanism.一种用于分析米氏机制速率常数的热变方法。
Biochem J. 1982 Oct 1;207(1):179-81. doi: 10.1042/bj2070179.
3
A comparison of 31P-NMR saturation transfer and isotope-exchange measurements of creatine kinase kinetics in vitro.体外肌酸激酶动力学的31P-NMR饱和转移与同位素交换测量的比较。
Biochim Biophys Acta. 1984 Apr 27;786(1-2):18-24. doi: 10.1016/0167-4838(84)90148-1.
4
NMR spin exchange kinetics at equilibrium in membrane transport and enzyme systems.膜运输和酶系统中平衡状态下的核磁共振自旋交换动力学。
J Theor Biol. 1983 Dec 21;105(4):569-89. doi: 10.1016/0022-5193(83)90220-5.
5
31P NMR spin-transfer in the phosphoglyceromutase reaction.磷酸甘油酸变位酶反应中的31P核磁共振自旋转移
Eur J Biochem. 1984 Sep 17;143(3):643-9. doi: 10.1111/j.1432-1033.1984.tb08417.x.
6
Kinetics of isotope exchange at equilibrium for a one substrate-one product enzyme mechanism.单底物-单产物酶机制在平衡状态下的同位素交换动力学。
J Theor Biol. 1973 Nov 5;42(1):55-62. doi: 10.1016/0022-5193(73)90148-3.

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.

DOI:10.1042/bj2440247
PMID:3663116
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147980/
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。