PURIFICATION OF NITRIC-OXIDE SYNTHASE FROM BOVINE BRAIN - IMMUNOLOGICAL CHARACTERIZATION AND TISSUE DISTRIBUTION

被引：79

作者：

OHSHIMA, H ^{[1
]}

OGUCHI, S ^{[1
]}

ADACHI, H ^{[1
]}

IIDA, S ^{[1
]}

SUZUKI, H ^{[1
]}

SUGIMURA, T ^{[1
]}

ESUMI, H ^{[1
]}

机构：

[1] NATL CANC CTR,RES INST,DIV BIOCHEM,1-1 TSUKIJI 5-CHOME,CHUO KU,TOKYO 104,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 183卷 / 01期

关键词：

D O I：

10.1016/0006-291X(92)91634-3

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：

Nitric oxide (NO) synthase (EC 1.14.23) was purified to homogeneity from bovine cerebrum. The molecular weight of NO synthase was estimated to be 150 kDa by both SDS PAGE and gel filtration at high salt concentration. For activity, the enzyme required NADPH, Ca2+, calmodulin and tetrahydrobiopterin as cofactors. Rabbit polyclonal antibody to bovine brain NO synthase reacted with 150 kDa NO synthase in various bovine and rat organs, including the brain, pituitary and adrenal glands, but not with that in stimulated macrophages, indicating that there are at least two immunologically distinct NO synthases. © 1992.

引用

页码：238 / 244

页数：7

共 15 条

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