Purification and characterization of mouse liver xanthine oxidase

G Carpani; M Racchi; P Ghezzi; M Terao; E Garattini

doi:10.1016/0003-9861(90)90487-j

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.

Authors

G Carpani¹, M Racchi, P Ghezzi, M Terao, E Garattini

Affiliation

¹ Molecular Biology Unit, Centro Daniela e Catullo Borgomainerio, Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy.

PMID: 2350174
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