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变构及其他复杂酶机制的配体结合和初速率数据的定量分析。

The quantitative analysis of ligand binding and initial-rate data for allosteric and other complex enzyme mechanisms.

作者信息

Bardsley W G

出版信息

Biochem J. 1976 Jan 1;153(1):101-17. doi: 10.1042/bj1530101.

Abstract
  1. The eight methods for plotting enzyme kinetic data are classified and analysed, and it is shown how, in each case, it is only possible to obtain quantitative data on the coefficients of the lowest- and highest-degree terms in the rate equation. 2. The combinations of coefficients that are accessible experimentally from limiting slopes and intercepts at both low and high substrate concentration are stated for all the graphical methods and the precise effects of these on curve shape in different spaces is discussed. 3. Ambiguities arising in the analysis of complex curves and certain special features are also investigated. 4. Four special ordering functions are defined and investigated and it is shown how knowledge of these allows a complete description of all possible complex curve shapes.
摘要
  1. 对绘制酶动力学数据的八种方法进行了分类和分析,并说明了在每种情况下,如何仅能获得速率方程中最低次项和最高次项系数的定量数据。2. 针对所有图形方法,阐述了可从低底物浓度和高底物浓度下的极限斜率与截距实验获得的系数组合,并讨论了这些组合在不同空间中对曲线形状的精确影响。3. 还研究了复杂曲线分析中出现的模糊性和某些特殊特征。4. 定义并研究了四种特殊的排序函数,并说明了对这些函数的了解如何能完整描述所有可能的复杂曲线形状。

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Dose any enzyme follow the Michaelis-Menten equation?有任何酶遵循米氏方程吗?
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