Literature DB >> 1575708

The error in the Michaelis-Menten equation when substrate depletion by binding to the enzyme is not taken into account.

K P Heirwegh, M Vermeir.   

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Year:  1992        PMID： 1575708      PMCID： PMC1131084          DOI： 10.1042/bj2830623

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


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  4 in total

1.  Determination of dissociation and Michaelis constants at near-equal enzyme-substrate concentrations.

Authors:  G D Smith; R Eisenthal; R Harrison
Journal:  Anal Biochem       Date:  1977-05-01       Impact factor: 3.365

2.  Liposomes as carriers of poorly water-soluble substrates: linear modelling of membrane systems with catalytic or binding sites of different facedness. Significance of experimental membrane partition coefficients and of kinetic and equilibrium parameters.

Authors:  K P Heirwegh; J A Meuwissen; M Vermeir; H De Smedt
Journal:  Biochem J       Date:  1988-08-15       Impact factor: 3.857

3.  Kinetic behavior at high enzyme concentrations. Magnitude of errors of Michelis-Menten and other approximations.

Authors:  S Cha
Journal:  J Biol Chem       Date:  1970-09-25       Impact factor: 5.157

4.  The determination of binding parameters when the total and free substrate concentrations are not approximately equal.

Authors:  N Gains
Journal:  Biochem J       Date:  1979-06-01       Impact factor: 3.857
  4 in total

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