变构酶正协同性和负协同性的测定，以及米氏常数（MWC）和齐变模型（KNF）的S形曲线和非线性双倒数图的解释。 - Suppr

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The determination of positive and negative co-operativity with allosteric enzymes and the interpretation of sigmoid curves and non-linear double reciprocal plots for the MWC and KNF models.

作者信息

Bardsley W G, Waight R D

出版信息

J Theor Biol. 1978 Jan 20;70(2):135-56. doi: 10.1016/0022-5193(78)90343-0.

DOI:10.1016/0022-5193(78)90343-0

PMID:633912

Abstract

摘要

相似文献

The determination of positive and negative co-operativity with allosteric enzymes and the interpretation of sigmoid curves and non-linear double reciprocal plots for the MWC and KNF models.变构酶正协同性和负协同性的测定，以及米氏常数（MWC）和齐变模型（KNF）的S形曲线和非线性双倒数图的解释。

J Theor Biol. 1978 Jan 20;70(2):135-56. doi: 10.1016/0022-5193(78)90343-0.

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Co-operativity and the methods of plotting binding and steady-state kinetic data.协同性以及绘制结合和稳态动力学数据的方法。

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Validity of transfer-function representation of input-output relation in allosteric models.变构模型中输入-输出关系的传递函数表示的有效性。

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Kinetic manifestations of allosteric interactions in models of regulatory enzymes with "indirect" co-operativity.具有“间接”协同性的调节酶模型中变构相互作用的动力学表现

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Subunit coupling and kinetic co-operativity of polymeric enzymes. Amplification, attenuation and inversion effects.多聚酶的亚基偶联与动力学协同性。放大、衰减及反转效应。

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An analysis of non-linear Eadie-Hofstee-Scatchard representations of ligand-binding and initial-rate data for allosteric and other complex enzyme mechanisms.对变构及其他复杂酶机制的配体结合和初速率数据的非线性伊迪-霍夫斯泰-斯卡查德表示法的分析。

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A model for the allosteric regulation of pH-sensitive enzymes.一种pH敏感酶变构调节的模型。

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Letter: Kinetic negative co-operativity in the allosteric model of Monod, Wyman and Changeux.

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引用本文的文献

The probability that complex enzyme kinetic curves can be caused by activators of inhibitors.由激活剂或抑制剂引起复杂酶动力学曲线的可能性。

Biochem J. 1981 Jun 1;195(3):589-601. doi: 10.1042/bj1950589.

Deviations from Michaelis-Menten kinetics. Computation of the probabilities of obtaining complex curves from simple kinetic schemes.偏离米氏动力学。从简单动力学机制计算获得复杂曲线的概率。

Biochem J. 1981 Jan 1;193(1):339-52. doi: 10.1042/bj1930339.

Use of the F test for determining the degree of enzyme-kinetic and ligand-binding data. A Monte Carlo simulation study.使用F检验确定酶动力学和配体结合数据的程度。一项蒙特卡罗模拟研究。

Biochem J. 1983 Apr 1;211(1):23-34. doi: 10.1042/bj2110023.

Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.与米氏动力学的偏差。简单动力学机制出现复杂曲线的可能性以及对乙酰胆碱酯酶、酸性磷酸酶、腺苷脱氨酶、芳基硫酸酯酶、苄胺氧化酶、胰凝乳蛋白酶、延胡索酸酶、半乳糖脱氢酶、β-半乳糖苷酶、乳酸脱氢酶、过氧化物酶和黄嘌呤氧化酶的实验数据进行计算机拟合。

Biochem J. 1980 Jun 1;187(3):739-65. doi: 10.1042/bj1870739.

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