Purification and Characterization of Mouse Liver Xanthine Oxidase

Arch Biochem Biophys. 1990 Jun;279(2):237-41. doi: 10.1016/0003-9861(90)90487-j.

Abstract

Xanthine oxidase (EC 1.1.3.22) is purified to homogeneity from mouse liver after induction with bacterial lipopolysaccharide. The enzyme has an apparent molecular weight of 300,000 in its native state and it is suggested to be constituted of two identical subunits of Mr 150,000 each. The isoelectric point is 6.7 and the apparent Km value for xanthine is 3.4 microM. The amino acid composition of mouse xanthine oxidase is quite similar to that of Drosophila xanthine dehydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Enzyme Induction / drug effects
  • Lipopolysaccharides / pharmacology
  • Liver / enzymology*
  • Male
  • Mice
  • Molecular Weight
  • Spectrum Analysis
  • Xanthine Oxidase / isolation & purification*

Substances

  • Amino Acids
  • Lipopolysaccharides
  • Xanthine Oxidase