PURIFICATION AND CHARACTERIZATION OF MOUSE-LIVER XANTHINE-OXIDASE

被引：28

作者：

CARPANI, G ^{[1
]}

RACCHI, M ^{[1
]}

GHEZZI, P ^{[1
]}

TERAO, M ^{[1
]}

GARATTINI, E ^{[1
]}

机构：

[1] MARIO NEGRI INST PHARMACOL RES,CTR DANIELA & CATULLO BORGOMAINERIO,MOLEC BIOL UNIT,I-20157 MILAN,ITALY

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1990年 / 279卷 / 02期

关键词：

D O I：

10.1016/0003-9861(90)90487-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 μm. The amino acid composition of mouse xanthine oxidase is quite similar to that of Drosophila xanthine dehydrogenase. © 1990.

引用

页码：237 / 241

页数：5

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