Literature DB >> 1218083

The nature of experimental error in enzyme kinetic measurments.

A C Storer, M G Darlison, A Cornish-Bowden.   

Abstract

The nature of experimental error in the determination of initial velocities of enzyme-catalysed reactions was investigated. No support was found for the generalization that such velocities should be homogeneous in variance. Instead the variance increased with the velocity in all of the cases studied. The weighting of sets of replicate observations according to their sample variances was tested in simulated experiments and found to give unacceptable results. It was practicable to decide on the best weighting scheme by examining the variability of the deviations from fitted curves, provided that the number of observations was large enough.

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Year:  1975        PMID: 1218083      PMCID: PMC1172366          DOI: 10.1042/bj1510361

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  14 in total

1.  Parameter estimation and enzyme kinetic models.

Authors:  J G. Reich
Journal:  FEBS Lett       Date:  1970-08-31       Impact factor: 4.124

2.  A COMPARISON OF ESTIMATES OF MICHAELIS-MENTEN KINETIC CONSTANTS FROM VARIOUS LINEAR TRANSFORMATIONS.

Authors:  J E DOWD; D S RIGGS
Journal:  J Biol Chem       Date:  1965-02       Impact factor: 5.157

3.  Statistical estimations in enzyme kinetics.

Authors:  G N WILKINSON
Journal:  Biochem J       Date:  1961-08       Impact factor: 3.857

4.  Statistical analysis of enzymic steady-state rate data.

Authors:  G JOHANSEN; R LUMRY
Journal:  C R Trav Lab Carlsberg       Date:  1961

5.  A general method for the quantitative determination of saturation curves for multisubunit proteins.

Authors:  A Cornish-Bowden; D E Koshland
Journal:  Biochemistry       Date:  1970-08-18       Impact factor: 3.162

6.  The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme.

Authors:  A C Storer; A Cornish-Bowden
Journal:  Biochem J       Date:  1974-07       Impact factor: 3.857

7.  Normalization in the fitting of data by iterative methods. Application to tracer kinetics and enzyme kinetics.

Authors:  J H Ottaway
Journal:  Biochem J       Date:  1973-07       Impact factor: 3.857

8.  Statistical considerations in the estimation of enzyme kinetic parameters by the direct linear plot andother methods.

Authors:  A Cornish-Bowden; R Eisenthal
Journal:  Biochem J       Date:  1974-06       Impact factor: 3.857

9.  A general strategy for parameter estimation from isosteric and allosteric-kinetic data and binding measurements.

Authors:  J G Reich; G Wangermann; M Falck; K Rohde
Journal:  Eur J Biochem       Date:  1972-04-11

10.  Further properties and possibel mechanism of action of adenosine 5'-triphosphate-D-glucose 6-phosphotransferase from rat liver.

Authors:  M J Parry; D G Walker
Journal:  Biochem J       Date:  1967-11       Impact factor: 3.857

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  13 in total

1.  Analysis of algebraic weighted least-squares estimators for enzyme parameters.

Authors:  M E Jones
Journal:  Biochem J       Date:  1992-12-01       Impact factor: 3.857

2.  Steady-state kinetic studies of the negative co-operativity and flip-flop mechanism for Escherichia coli alkaline phosphatase.

Authors:  R D Waight; P Leff; W G Bardsley
Journal:  Biochem J       Date:  1977-12-01       Impact factor: 3.857

3.  Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase.

Authors:  A C Storer; A Cornish-Bowden
Journal:  Biochem J       Date:  1977-07-01       Impact factor: 3.857

4.  Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.

Authors:  B Mannervik; I Jakobson; M Warholm
Journal:  Biochem J       Date:  1986-05-01       Impact factor: 3.857

5.  Analytical methods for fitting integrated rate equations. A discontinuous assay.

Authors:  E A Boeker
Journal:  Biochem J       Date:  1987-07-01       Impact factor: 3.857

6.  Use of the F test for determining the degree of enzyme-kinetic and ligand-binding data. A Monte Carlo simulation study.

Authors:  F J Burguillo; A J Wright; W G Bardsley
Journal:  Biochem J       Date:  1983-04-01       Impact factor: 3.857

7.  Comparison of several non-linear-regression methods for fitting the Michaelis-Menten equation.

Authors:  L Matyska; J Kovár
Journal:  Biochem J       Date:  1985-10-01       Impact factor: 3.857

8.  Application of jackknife procedures to inter-experiment comparisons of parameter estimates for the Michaelis-Menten equation.

Authors:  L Oppenheimer; T P Capizzi; G T Miwa
Journal:  Biochem J       Date:  1981-09-01       Impact factor: 3.857

9.  Fitting of enzyme kinetic data without prior knowledge of weights.

Authors:  A Cornish-Bowden; L Endrenyi
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857

10.  Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart.

Authors:  C L McMinn; J H Ottaway
Journal:  Biochem J       Date:  1977-03-01       Impact factor: 3.857

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