Purification and characterization of mouse liver xanthine oxidase

Giovanna Carpani, Marco Racchi, Pietro Ghezzi, Mineko Terao, Enrico Garattini

Research output: Contribution to journalArticlepeer-review


Xanthine oxidase (EC 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 μm. The amino acid composition of mouse xanthine oxidase is quite similar to that of Drosophila xanthine dehydrogenase.

Original languageEnglish
Pages (from-to)237-241
Number of pages5
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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