Purification of a Ca2+/calmodulin‐dependent nitric oxide synthase from porcine cerebellum

FEBS Letters

Böhme, Eycke¹  John, Mathias¹  Mayer, Bernd¹ 

[1] Institut für Pharmakologie, Freie Universität Berlin, Thielallee 67-73, D-1000 Berlin 33, Germany

关键词: Nitric oxide synthase;    Ca2+;    Calmodulin;    Tetrahydrobiopterin;    Guanylyl cyclase;    NADPH;   

DOI  :  10.1016/0014-5793(90)80848-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown