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1
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。
Biochem J. 1978 May 1;171(2):501-4. doi: 10.1042/bj1710501.
2
Kinetic co-operativity of monomeric mnemonical enzymes. The significance of the kinetic Hill coefficient.单体记忆酶的动力学协同性。动力学希尔系数的意义。
Eur J Biochem. 1985 Nov 4;152(3):557-64. doi: 10.1111/j.1432-1033.1985.tb09231.x.
3
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。
J Theor Biol. 1985 Dec 21;117(4):633-49. doi: 10.1016/s0022-5193(85)80244-7.
4
Rates of reactions catalysed by a dimeric enzyme. Effects of the reaction scheme and the kinetic parameters on co-operativity.二聚体酶催化的反应速率。反应机制和动力学参数对协同性的影响。
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5
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。
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6
Co-operativity in monomeric enzymes.单体酶中的协同性。
J Theor Biol. 1987 Jan 7;124(1):1-23. doi: 10.1016/s0022-5193(87)80248-5.
7
Evaluation of Hill slopes and Hill coefficients when the saturation binding or velocity is not known.在饱和结合或反应速度未知时对Hill斜率和Hill系数的评估。
Eur J Biochem. 1975 Feb 21;51(2):317-28. doi: 10.1111/j.1432-1033.1975.tb03931.x.
8
Absence of positive co-operativity in the binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin to its cytosolic receptor protein.2,3,7,8-四氯二苯并对二恶英与其胞质受体蛋白结合时不存在正协同性。
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Potential misconceptions arising from the application of enzyme kinetic equations to ligand-receptor systems at equilibrium.在平衡状态下将酶动力学方程应用于配体-受体系统时可能产生的误解。
Can J Physiol Pharmacol. 1988 Apr;66(4):342-9. doi: 10.1139/y88-059.
10
Analysis of one-component saturable systems such as ligand binding, enzyme kinetic, uptake, and transport data.对单组分可饱和系统的分析，如配体结合、酶动力学、摄取和转运数据。
J Pharmacol Methods. 1986 Aug;16(1):1-22. doi: 10.1016/0160-5402(86)90025-2.

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A hierarchical approach to cooperativity in macromolecular and self-assembling binding systems.一种用于大分子和自组装结合系统协同性的分层方法。
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The exponential model for a regulatory enzyme. An interpretation of the linear free-energy relationship.调节酶的指数模型。线性自由能关系的一种解释。
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6
A computer program for enzyme kinetics that combines model discrimination, parameter refinement and sequential experimental design.一种用于酶动力学的计算机程序，它结合了模型判别、参数优化和序贯实验设计。
Biochem J. 1986 Sep 15;238(3):855-62. doi: 10.1042/bj2380855.
7
Patterns of apparent co-operativity in a simple random non-equilibrium enzyme--substrate--modifier mechanism. Comparison with equilibrium allosteric models.简单随机非平衡酶-底物-调节剂机制中的表观协同模式。与平衡别构模型的比较。
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Pyruvate kinase. Classes of regulatory isoenzymes in mammalian tissues.丙酮酸激酶。哺乳动物组织中的调节性同工酶类别。
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Models for cooperative effects in proteins containing subunits. Effects of two interacting ligands.含亚基蛋白质中协同效应的模型。两个相互作用配体的效应。
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A new plot for allosteric phenomena.变构现象的一种新模型。
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Factorability of the allosteric binding polynomial and graphical manifestations of cooperativity in third degree saturation functions.变构结合多项式的可分解性及三级饱和度函数中协同性的图形表现
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The relationship between co-operativity coefficients, factorability of the allosteric binding polynomial and curve shape.协同系数、别构结合多项式的可分解性与曲线形状之间的关系。
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协同性以及绘制结合和稳态动力学数据的方法。

Co-operativity and the methods of plotting binding and steady-state kinetic data.

作者信息

Whitehead E P

出版信息

Biochem J. 1978 May 1;171(2):501-4. doi: 10.1042/bj1710501.

DOI:10.1042/bj1710501
PMID:656060
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1183983/
Abstract

The features that distinguish positive from negative co-operativity in double-reciprocal Eadie-Hofstee-Scatchard and Hanes plots, often incorrectly stated to be the sign of curvature or second derivatives, are explained. It is shown how to determine the 'Hill exponent' and interaciton free energies from curves in these plots, and in the simple plot of ligand binding or velocity against free ligand or substrate concentration. New types of plots, where the kind of co-operative behaviour is more obvious than in the traditional ones, are proposed.

摘要

解释了双倒数伊迪-霍夫斯泰-斯卡查德图和黑尼斯图中区分正协同性和负协同性的特征，这些特征常被错误地表述为曲率或二阶导数的符号。展示了如何从这些图中的曲线以及配体结合或速度对游离配体或底物浓度的简单图中确定“希尔指数”和相互作用自由能。还提出了新型的图，其中协同行为的类型比传统图中更明显。