| Literature DB >> 1724623 |
J A Mitchell1, H Sheng, U Förstermann, F Murad.
Abstract
Tissue homogenates prepared from rat anococcygeus muscle converted L-arginine to L-citrulline indicating the presence of nitric oxide (NO) synthase. NO synthase activity was also found in crude and partially-purified soluble and particulate fractions prepared from the homogenates. Both soluble and particulate NO synthase were dependent on NADPH, 5,6,7,8-tetrahydrobiopterin and calcium, and inhibited by NG-nitro-L-arginine. Tissue homogenates or crude cytosolic and membrane fractions from rat vas deferens, which does not contain NO releasing non-adrenergic non-cholinergic neurones, had no NO synthase activity.Entities:
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Year: 1991 PMID: 1724623 PMCID: PMC1908579 DOI: 10.1111/j.1476-5381.1991.tb12422.x
Source DB: PubMed Journal: Br J Pharmacol ISSN: 0007-1188 Impact factor: 8.739