Literature DB >> 7305951

Fitting of enzyme kinetic data without prior knowledge of weights.

A Cornish-Bowden, L Endrenyi.   

Abstract

A method is described for fitting equations to enzyme kinetic data that requires minimal assumptions about the error structure of the data. The dependence of the variances on the velocities is not assumed, but is deduced from internal evidence in the data. The effect of very bad observations ('outliers') is mitigated by decreasing the weight of observations that give large deviations from the fitted equation. The method works well in a wide range of circumstances when applied to the Michaelis-Menten equation, but it is not limited to this equation. It can be applied to most of the equations in common use for the analysis of steady-state enzyme kinetics. It has been implemented as a computer program that can fit a wide variety of equations with two, three or four parameters and two or three variables.

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Year:  1981        PMID: 7305951      PMCID: PMC1162696          DOI: 10.1042/bj1931005

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


  8 in total

1.  A computer program for fitting and statistically analyzing initial rate data applied to bovine hexokinase type III isozyme.

Authors:  D B Siano; J W Zyskind; H J Fromm
Journal:  Arch Biochem Biophys       Date:  1975-10       Impact factor: 4.013

2.  The nature of experimental error in enzyme kinetic measurments.

Authors:  A C Storer; M G Darlison; A Cornish-Bowden
Journal:  Biochem J       Date:  1975-11       Impact factor: 3.857

3.  Error structure of enzyme kinetic experiments. Implications for weighting in regression analysis of experimental data.

Authors:  P Askelöf; M Korsfeldt; B Mannervik
Journal:  Eur J Biochem       Date:  1976-10-01

4.  The nature of the random experimental error encountered when acetylcholine hydrolase and alcohol dehydrogenase are assayed.

Authors:  I A Nimmo; S F Mabood
Journal:  Anal Biochem       Date:  1979-04-15       Impact factor: 3.365

5.  Evaluation of distribution-free confidence limits for enzyme kinetic parameters.

Authors:  A Cornish-Bowden; W R Porter; W F Trager
Journal:  J Theor Biol       Date:  1978-09-21       Impact factor: 2.691

6.  Estimation of Michaelis constant and maximum velocity from the direct linear plot.

Authors:  A Cornish-Bowden; R Eisenthal
Journal:  Biochim Biophys Acta       Date:  1978-03-14

Review 7.  Current trends in the estimation of Michaelis-Menten parameters.

Authors:  G L Atkins; I A Nimmo
Journal:  Anal Biochem       Date:  1980-05-01       Impact factor: 3.365

8.  Statistical analysis of enzyme kinetic data.

Authors:  W W Cleland
Journal:  Methods Enzymol       Date:  1979       Impact factor: 1.600

  8 in total
  14 in total

1.  Implications for clinical pharmacodynamic studies of the statistical characterization of an in vitro antiproliferation assay.

Authors:  L M Levasseur; H Faessel; H K Slocum; W R Greco
Journal:  J Pharmacokinet Biopharm       Date:  1998-12

2.  The effect of temperature on biochemical and molecular properties of Drosophila alcohol dehydrogenase.

Authors:  K C McElfresh; J F McDonald
Journal:  Biochem Genet       Date:  1986-12       Impact factor: 1.890

3.  Dihydropteridine reductase from Escherichia coli.

Authors:  S G Vasudevan; D C Shaw; W L Armarego
Journal:  Biochem J       Date:  1988-10-15       Impact factor: 3.857

4.  Robust regression of enzyme kinetic data.

Authors:  A Cornish-Bowden; L Endrenyi
Journal:  Biochem J       Date:  1986-02-15       Impact factor: 3.857

5.  Pharmacokinetic parameter estimates from several least squares procedures: superiority of extended least squares.

Authors:  L B Sheiner; S L Beal
Journal:  J Pharmacokinet Biopharm       Date:  1985-04

6.  Km and kcat. values for [6,6,7,7-2H]7,8(6H)-dihydropterin and 2,6-diamino-5-iminopyrimidin-4-one with dihydropteridine reductase.

Authors:  W L Armarego; D Randles; H Taguchi
Journal:  Biochem J       Date:  1983-05-01       Impact factor: 3.857

7.  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

8.  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

9.  Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.

Authors:  J Kovár; J Plocek
Journal:  Biochem J       Date:  1986-04-15       Impact factor: 3.857

10.  Temperature-related kinetic differentiation of glucosephosphate isomerase alleloenzymes isolated from the blue mussel, Mytilus edulis.

Authors:  J G Hall
Journal:  Biochem Genet       Date:  1985-10       Impact factor: 1.890

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