Literature DB >> 7396820

New relations for activity analysis of associating enzymes.

J C Thomes, J Archambault De Vençay, R Julien.   

Abstract

New relations for catalytic-activity analysis are proposed for simple association/dissociation equilibria between the mono- and oligo-meric forms of enzymes in the case where these equilibria evolve very slowly in comparison with the binding of the substrates. This analysis of activity versus total enzyme concentration leads rapidly to information, complementary to that given by physico-chemical methods, on specific activities, the degree of polymerization of the enzyme forms and on their dissociation constants.

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Year:  1980        PMID: 7396820      PMCID: PMC1161359          DOI: 10.1042/bj1850339

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


  11 in total

1.  Polysteric linkage.

Authors:  A Colosimo; M Brunori; J Wyman
Journal:  J Mol Biol       Date:  1976-01-05       Impact factor: 5.469

2.  A theoretical study of the binding of small molecules to a polymerizing protein system. A model for allosteric effects.

Authors:  L W Nichol; W J Jackson; D J Winzor
Journal:  Biochemistry       Date:  1967-08       Impact factor: 3.162

3.  The theoretical analysis of kinetic behaviour of "hysteretic" allosteric enzymes. IV. Kinetics of dissociation-association processes of allosteric enzymes.

Authors:  B I Kurganov
Journal:  J Theor Biol       Date:  1977-10-21       Impact factor: 2.691

4.  The theoretical analysis of kinetic behaviour of kinetic behaviour of "hysteretic" allosteric enzymes. III. Dissociating and associating enzyme systems in which the rate of installation of equilibrium between the oligomeric forms in comparable to that of enzymatic reaction.

Authors:  B I Kurganov; A K Dorozhko; Z S Kagan; V A Yakovlev
Journal:  J Theor Biol       Date:  1976-08-07       Impact factor: 2.691

5.  The theoretical analysis of kinetic behaviour of "hysteretic" allosteric enzymes. II. The dissociating and associating enzymic systems in which the rate of installation of equilibrium between the oligomeric forms is small in comparison with that of enzymatic reaction.

Authors:  B I Kurganov; A I Dorozhko; Z S Kagan; V A Yakovlev
Journal:  J Theor Biol       Date:  1976-08-07       Impact factor: 2.691

6.  Cooperativity in associating proteins. Monomer-dimer equilibrium coupled to ligand binding.

Authors:  A Levitzki; J Schlessinger
Journal:  Biochemistry       Date:  1974-12-03       Impact factor: 3.162

7.  Cooperative interactions and determination of protein association-dissociation equilibria. Hemerythrin.

Authors:  M H Klapper; I M Klotz
Journal:  Biochemistry       Date:  1968-01       Impact factor: 3.162

8.  Phenylalanyl-tRNA synthetase of the human placenta. Evidence for different enzymatic forms in equilibrium.

Authors:  J Archambault de Vencay; J C Thomes; R Julien
Journal:  FEBS Lett       Date:  1978-05-01       Impact factor: 4.124

9.  Treatment of enzyme kinetic data. II. The multisite case: comparison of allosteric models and a possible new mechanism.

Authors:  C Frieden
Journal:  J Biol Chem       Date:  1967-09-25       Impact factor: 5.157

10.  [Methionyl-tRNA synthetase from wheat embryo: dissociation into subunits (author's transl)].

Authors:  P Chazal; J C Thomes; R Julien
Journal:  Eur J Biochem       Date:  1977-03-01
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