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酶动力学数据误差结构测定中的残差分析。对食蟹猴磷酸果糖激酶的模拟实验与观察。

Residual analysis in determining the error structure in enzyme kinetic data. Simulation experiments and observations on Carcinus maenas phosphofructokinase.

作者信息

Little D I, Poat P C, Giles I G

出版信息

Eur J Biochem. 1982 Jun;124(3):499-505. doi: 10.1111/j.1432-1033.1982.tb06621.x.

DOI:10.1111/j.1432-1033.1982.tb06621.x
PMID:6213409
Abstract

The nature of the experimental error in the initial velocities of an enzyme-catalysed reaction is required if meaningful least-squares regression is to be applied. When a rate equation more complex that that of Michaelis and Menten is to be solved least-squares techniques are the method of choice and so determination of the error structure becomes mandatory. The use of residual analysis and Tukey's T statistics to determine the weights to use are described. This method has the advantage of requiring no additional experimentation over that required for the primary investigation. Using data obtained for Carcinus maenas phosphofructokinase the variance was found to increase with velocity and was approximated by either an empirical power function, var (vi) alpha vi1.8 or by the function, var (vi) alpha 0.007 + vi2. The latter function is preferred and suggests that the data contains both a constant absolute error and a constant percentage error component.

摘要

如果要应用有意义的最小二乘回归,就需要了解酶催化反应初速度实验误差的性质。当要求解比米氏方程更复杂的速率方程时,最小二乘技术是首选方法,因此确定误差结构就变得必不可少。文中描述了如何使用残差分析和图基T统计量来确定权重。这种方法的优点是,除了初步研究所需的实验外,不需要额外的实验。利用从食蟹猴磷酸果糖激酶获得的数据,发现方差随速度增加,并且可以用经验幂函数var(vi)∝vi1.8或函数var(vi)∝0.007 + vi2来近似。后一种函数更可取,表明数据包含恒定的绝对误差和恒定的百分比误差成分。

相似文献

1
Residual analysis in determining the error structure in enzyme kinetic data. Simulation experiments and observations on Carcinus maenas phosphofructokinase.酶动力学数据误差结构测定中的残差分析。对食蟹猴磷酸果糖激酶的模拟实验与观察。
Eur J Biochem. 1982 Jun;124(3):499-505. doi: 10.1111/j.1432-1033.1982.tb06621.x.
2
An investigation of the error structure in the initial-rate data of common-shore-crab (Carcinus maenas) phosphofructokinase.
Biochem Soc Trans. 1980 Oct;8(5):560-1. doi: 10.1042/bst0080560.
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Product-inhibition studies on phosphofructokinase isolated from the muscle of the common shore crab (Carcinus maenas).
Biochem Soc Trans. 1980 Oct;8(5):561-2. doi: 10.1042/bst0080561.
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A kinetic study on phosphofructokinase isolated from the muscle of Carcinus maenas (the common shore crab) [proceedings].
Biochem Soc Trans. 1980 Feb;8(1):142-3. doi: 10.1042/bst0080142.
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Determination of the best-fit values of kinetic parameters of the Michaelis-Menten equation by the method of least squares with the Taylor expansion.通过泰勒展开的最小二乘法确定米氏方程动力学参数的最佳拟合值。
J Biochem. 1976 Sep;80(3):547-55. doi: 10.1093/oxfordjournals.jbchem.a131310.
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Error structure of enzyme kinetic experiments. Implications for weighting in regression analysis of experimental data.酶动力学实验的误差结构。对实验数据回归分析中加权的影响。
Eur J Biochem. 1976 Oct 1;69(1):61-7. doi: 10.1111/j.1432-1033.1976.tb10858.x.
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An investigation into the apparent inhibition by arginine phosphate of the activity of Carcinus maenas type-M pyruvate kinase.关于磷酸精氨酸对海蟹型-M丙酮酸激酶活性的明显抑制作用的研究。
Biochim Biophys Acta. 1980 Jun 13;613(2):410-9. doi: 10.1016/0005-2744(80)90095-9.
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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.
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Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei.布氏锥虫磷酸果糖激酶催化反应的动力学研究
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[Simulation of the kinetics of oligomeric enzymes as illustrated by phosphofructokinase. I. General analysis of experimental data and the choice of an adequate model].
Mol Biol (Mosk). 1987 May-Jun;21(3):820-30.

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