Exact and user-friendly kinetic analysis of the two-step rapid equilibrium Michaelis-Menten mechanism

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2 Scopus citations

Abstract

Most enzyme kinetic experiments are carried out under pseudo-first-order conditions, that is, when one of the reactant species (the enzyme or the substrate) is in a large excess of the other species. More accurate kinetic information about the system can be gained without the restrictions of the pseudo-first-order conditions. We present a practical and general method of analysis of the common two-step rapid equilibrium Michaelis-Menten mechanism. The formalism is exact in that it does not involve any other approximations such as the steady-state, limitations on the reactant concentrations or on reaction times. We apply this method to the global analysis of kinetic progress curves for bovine alkaline phosphatase assays carried out under both pseudo-first-order and pseudo-second-order conditions.

Original languageEnglish
Pages (from-to)276-279
Number of pages4
JournalAnalytical Biochemistry
Volume387
Issue number2
DOIs
StatePublished - Apr 15 2009

Keywords

  • Alkaline phosphatase
  • Kinetic analysis
  • Michaelis-Menten
  • Progress curve
  • Rapid equilibrium
  • Rate law

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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