Literature DB >> 3593279

Theoretical analysis of a translocation-like model with saturable kinetics.

B Maïsterrena, L J Blum, P R Coulet.   

Abstract

A theoretical analysis of the initial rates of product appearance in both compartments of a specifically designed diffusion cell separated by an asymmetrical enzyme membrane is presented. Variable substrate concentrations and different substrate diffusional limitations were considered. Our analysis shows that, under specific conditions, not only a product accumulation occurs in the compartment opposite to that in which the reaction takes place, but that substrate saturable kinetics can be obtained. These product translocation-like kinetics appear similar to those observed with translocation processes reported for biological situations. For such phenomena, a key role of the diffusion layer surrounding a bioactive surface is proposed.

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Year:  1987        PMID: 3593279      PMCID: PMC1147785          DOI: 10.1042/bj2420835

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


  3 in total

1.  Vectorial product concentration obtained with a permeable immobilized enzyme membrane. A new approach to the analysis of biological transport systems.

Authors:  B Maïsterrena; L J Blum; G Bardeletti; P R Coulet
Journal:  Biochem J       Date:  1986-05-01       Impact factor: 3.857

Review 2.  Translocations through natural membranes.

Authors:  P Mitchell
Journal:  Adv Enzymol Relat Areas Mol Biol       Date:  1967

Review 3.  A minimal hypothesis for membrane-linked free-energy transduction. The role of independent, small coupling units.

Authors:  H V Westerhoff; B A Melandri; G Venturoli; G F Azzone; D B Kell
Journal:  Biochim Biophys Acta       Date:  1984-12-17
  3 in total
  2 in total

1.  Compartmentalized system with membrane-bound glycerol kinase. Activity and product distribution versus asymmetrical substrate supply.

Authors:  A Girard; B Merchie; B Maïsterrena
Journal:  Biochem J       Date:  1991-03-15       Impact factor: 3.857

2.  Mimicked translocation of glucose and glucose 6-phosphate with artificial enzyme membranes.

Authors:  B Maïsterrena; P R Coulet
Journal:  Biochem J       Date:  1989-06-01       Impact factor: 3.857

  2 in total

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