Purification of a Ca2+/calmodulin‐dependent nitric oxide synthase from porcine cerebellum
- 17 December 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 277 (1-2), 215-219
- https://doi.org/10.1016/0014-5793(90)80848-d
Abstract
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, Ca 2+ -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 Ca 2+ /calmodulin and NADPH, largely dependent on tetrahydrobiopterin as a cofactor.This publication has 25 references indexed in Scilit:
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