PURIFICATION OF A CA-2+/CALMODULIN-DEPENDENT NITRIC-OXIDE SYNTHASE FROM PORCINE CEREBELLUM - COFACTOR-ROLE OF TETRAHYDROBIOPTERIN

被引：386

作者：

MAYER, B

JOHN, M

BOHME, E

机构：

[1] Institut für Pharmakologie, Freie Universität Berlin, D-1000 Berlin 33

来源：

FEBS LETTERS | 1990年 / 277卷 / 1-2期

关键词：

NITRIC OXIDE SYNTHASE; CA-2+; CALMODULIN; TETRAHYDROBIOPTERIN; GUANYLYL CYCLASE; NADPH;

D O I：

10.1016/0014-5793(90)80848-D

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：

L-Arginine-derived nitric oxide acts as an inter- and intracellular signal molecule with cytosolic guanylyl cyclase as the effector system. Two NO synthase isoenzymes are postulated: a cytokine-inducible enzyme in macrophages and a constitutive, Ca2+-regulated enzyme in various other cells. An NO synthase was isolated from porcine cerebellum by ammonium sulfate precipitation and affinity chromatography on 2',5'-ADP-Sepharose. The enzyme was identified as an NO synthase with a specific NO-chemiluminescence method and with purified cytosolic guanylyl cyclase as an NO-sensitive detection system. The purified NO synthase was, besides Ca2+/calmodulin and NADPH, largely dependent on tetrahydrobiopterin as a cofactor.

引用

页码：215 / 219

页数：5

共 28 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] ISOLATION OF NITRIC-OXIDE SYNTHETASE, A CALMODULIN-REQUIRING ENZYME [J].