Literature DB >> 1180901

Sigmoid curves, non-linear double-reciprocal plots and allosterism.

W G Bardsley, R E Childs.   

Abstract

1. The theory of plane curves was applied to the graphical methods used in enzyme kinetics and a mathematical analysis of the possible graph shapes is given. 2. The belief that allosterism can be inferred from steady-state data alone is subjected to criticism and the mathematical significance of sigmoid curves and non-linear double-reciprocal plots is explored. 3. It is suggested that the usual methods of interpreting steady-state kinetic data are often based on over-restrictive assumptions which prevent maximum utilization of the available data. 4. Methods for obtaining the degree of the rate equation from graph shapes obtained directly from initial-rate measurements and from replots of asymptotic behaviour as chi approach the level 0 and chi approach the level infinity are discussed. 5. Detailed proofs of the theorems given in the text have been deposited as Supplementary Publication SUP 50049 (10 pages) at the British Library (Lending Division), Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.

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Year:  1975        PMID: 1180901      PMCID: PMC1165625          DOI: 10.1042/bj1490313

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


  24 in total

1.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors:  J MONOD; J WYMAN; J P CHANGEUX
Journal:  J Mol Biol       Date:  1965-05       Impact factor: 5.469

2.  The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.

Authors:  W W CLELAND
Journal:  Biochim Biophys Acta       Date:  1963-02-12

3.  Kinetic formulations for enzymic reactions involving two substrates.

Authors:  J T WONG; C S HANES
Journal:  Can J Biochem Physiol       Date:  1962-06

4.  Transients and cooperativity. A slow transition model for relating transients and cooperative kinetics of enzymes.

Authors:  G R Ainslie; J P Shill; K E Neet
Journal:  J Biol Chem       Date:  1972-11-10       Impact factor: 5.157

Review 5.  Kinetics of allosteric enzymes.

Authors:  G G Hammes; C W Wu
Journal:  Annu Rev Biophys Bioeng       Date:  1974

6.  Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes.

Authors:  P C Engel; K Dalziel
Journal:  Biochem J       Date:  1969-12       Impact factor: 3.857

7.  Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase.

Authors:  A Conway; D E Koshland
Journal:  Biochemistry       Date:  1968-11       Impact factor: 3.162

8.  A model for the effects of binding and interaction energies on the kinetics of multivalent enzymes.

Authors:  H Moraal
Journal:  J Theor Biol       Date:  1972-11       Impact factor: 2.691

9.  A comparative study of some mechanisms describing interaction effects in a dimeric, two-substrate enzyme catalysed reaction.

Authors:  S Ainsworth
Journal:  J Theor Biol       Date:  1968-04       Impact factor: 2.691

10.  Comparison of experimental binding data and theoretical models in proteins containing subunits.

Authors:  D E Koshland; G Némethy; D Filmer
Journal:  Biochemistry       Date:  1966-01       Impact factor: 3.162

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  16 in total

1.  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

2.  Deviation from Michaelis-Menten kinetics for fumarase.

Authors:  M J Crabbe; W G Bardsley
Journal:  Biochem J       Date:  1976-08-01       Impact factor: 3.857

3.  A model for the allosteric regulation of pH-sensitive enzymes.

Authors:  J S Shindler; K F Tipton
Journal:  Biochem J       Date:  1977-11-01       Impact factor: 3.857

4.  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

5.  Dose any enzyme follow the Michaelis-Menten equation?

Authors:  C M Hill; R D Waight; W G Bardsley
Journal:  Mol Cell Biochem       Date:  1977-05-03       Impact factor: 3.396

6.  Abrupt transitions in kinetic plots: an artifact of plotting procedures.

Authors:  A Cornish-Bowden
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

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

Authors:  R Franco; M T Gavaldà; E I Canela
Journal:  Biochem J       Date:  1986-09-15       Impact factor: 3.857

8.  Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.

Authors:  W G Bardsley; P Leff; J Kavanagh; R D Waight
Journal:  Biochem J       Date:  1980-06-01       Impact factor: 3.857

9.  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

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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