Data di Pubblicazione:
1990
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.
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.
Tipologia CRIS:
1.1 Articolo in rivista
Elenco autori:
Carpani, G; Racchi, Marco; Ghezzi, P; Terao, M; Garattini, E.
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