Excess substrate inhibition of xanthine oxidase: a reexamination

Arch Biochem Biophys. 1993 Nov 1;306(2):415-9. doi: 10.1006/abbi.1993.1531.

Abstract

Xanthine oxidase has long been considered to be subject to inhibition by excess substrate. It is now shown that, although such inhibition can be seen in Tris or N,N-bis(2-hydroxyethyl)glycine buffers, earlier reports in which phosphate, pyrophosphate, or Veronal buffers were used were probably the result of a spectrophotometric artifact imposed by stray light in the incident beam.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Barbital / pharmacology
  • Buffers
  • Cattle
  • Female
  • Glycine / analogs & derivatives
  • Glycine / pharmacology
  • Kinetics
  • Mathematics
  • Milk / enzymology
  • Phosphates / pharmacology
  • Potassium Compounds / pharmacology
  • Regression Analysis
  • Tromethamine / pharmacology
  • Xanthine
  • Xanthine Oxidase / antagonists & inhibitors*
  • Xanthines / pharmacology*

Substances

  • Buffers
  • Phosphates
  • Potassium Compounds
  • Xanthines
  • Tromethamine
  • Xanthine
  • N,N-bis(2-hydroxyethyl)glycine
  • Barbital
  • potassium phosphate
  • Xanthine Oxidase
  • Glycine