Literature DB >> 3800965

A computer program for enzyme kinetics that combines model discrimination, parameter refinement and sequential experimental design.

R Franco, M T Gavaldà, E I Canela.   

Abstract

A method of model discrimination and parameter estimation in enzyme kinetics is proposed. The experimental design and analysis of the model are carried out simultaneously and the stopping rule for experimentation is deduced by the experimenter when the probabilities a posteriori indicate that one model is clearly superior to the rest. A FORTRAN77 program specifically developed for joint designs is given. The method is very powerful, as indicated by its usefulness in the discrimination between models. For example, it has been successfully applied to three cases of enzyme kinetics (a single-substrate Michaelian reaction with product inhibition, a single-substrate complex reaction and a two-substrate reaction). By using this method the most probable model and the estimates of the parameters can be obtained in one experimental session. The FORTRAN77 program is deposited as Supplementary Publication SUP 50134 (19 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1986) 233, 5.

Entities:  

Mesh:

Substances:

Year:  1986        PMID: 3800965      PMCID: PMC1147214          DOI: 10.1042/bj2380855

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


  21 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.  Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms.

Authors:  E P Whitehead
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

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

Authors:  W G Bardsley
Journal:  Biochem J       Date:  1976-01-01       Impact factor: 3.857

4.  The structure of steady-state enzyme kinetic equations: a graph-theoretical algorithm for obtaining conditions for reduction in degree by common-factor cancellation.

Authors:  E P Whitehead
Journal:  J Theor Biol       Date:  1979-10-07       Impact factor: 2.691

5.  Experimental designs for estimating the kinetic parameters for enzyme-catalysed reactions.

Authors:  R G Duggleby
Journal:  J Theor Biol       Date:  1979-12-21       Impact factor: 2.691

6.  A free derivative program for non-linear regression analysis of enzyme kinetics to be used on small computers.

Authors:  E I Canela
Journal:  Int J Biomed Comput       Date:  1984 Mar-Apr

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.  Relationships between the magnitude of Hill plot slopes, apparent binding constants and factorability of bindings polynomials and their Hessians.

Authors:  W G Bardsley; R Woolfson; J P Mazat
Journal:  J Theor Biol       Date:  1980-07-21       Impact factor: 2.691

9.  Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models.

Authors:  B Mannervik
Journal:  Methods Enzymol       Date:  1982       Impact factor: 1.600

10.  The probability that complex enzyme kinetic curves can be caused by activators of inhibitors.

Authors:  F Solano-Muñoz; W G Bardsley; K J Indge
Journal:  Biochem J       Date:  1981-06-01       Impact factor: 3.857

View more
  5 in total

1.  The molybdoenzymes xanthine oxidase and aldehyde oxidase contain fast- and slow-DTNB reacting sulphydryl groups.

Authors:  F Cabré; M Cascante; E I Canela
Journal:  J Protein Chem       Date:  1992-10

2.  Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven.

Authors:  A L Creagh; E Ong; E Jervis; D G Kilburn; C A Haynes
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

3.  Analysis of progress curves by simulations generated by numerical integration.

Authors:  C T Zimmerle; C Frieden
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

4.  Kinetic studies of chicken and turkey liver mitochondrial aspartate aminotransferase.

Authors:  M Cascante; A Cortés
Journal:  Biochem J       Date:  1988-03-15       Impact factor: 3.857

5.  Kinetic mechanism of chicken liver xanthine dehydrogenase.

Authors:  P Bruguera; A Lopez-Cabrera; E I Canela
Journal:  Biochem J       Date:  1988-01-01       Impact factor: 3.857

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.