Literature DB >> 886623

The relationship between co-operativity coefficients, factorability of the allosteric binding polynomial and curve shape.

W G Bardsley.   

Abstract

Mesh：

Year:  1977        PMID： 886623     DOI： 10.1016/0022-2836(77)90240-6

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  4 in total

1.  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

2.  Deviations from Michaelis-Menten kinetics. Computation of the probabilities of obtaining complex curves from simple kinetic schemes.

Authors:  F Solano-Muñoz; P B McGinlay; R Woolfson; W G Bardsley
Journal:  Biochem J       Date:  1981-01-01       Impact factor: 3.857

3.  Co-operativity and the methods of plotting binding and steady-state kinetic data.

Authors:  E P Whitehead
Journal:  Biochem J       Date:  1978-05-01       Impact factor: 3.857

4.  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
  4 in total

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