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  • Title: Potent inhibition of human neuronal nitric oxide synthase by N(G)-nitro-L-arginine methyl ester results from contaminating N(G)-nitro-L-arginine.
    Author: Furfine ES, Carbine K, Bunker S, Tanoury G, Harmon M, Laubach V, Sherman P.
    Journal: Life Sci; 1997; 60(20):1803-9. PubMed ID: 9150420.
    Abstract:
    N(G)-Nitro-L-arginine methyl ester (L-NAME), inhibits the three isozymes of nitric oxide synthase (NOS) in vitro and in vivo. The mechanism of NOS inhibition by L-NAME is uncertain. L-NAME was a time-dependent inhibitor of neuronal NOS (nNOS). Concommitantly, L-NAME was hydrolyzed, non-enzymatically, to N(G)-Nitro-L-arginine (L-NA) during the enzyme assay. The time-dependent inhibition of nNOS by L-NAME was the result of this time-dependent formation of L-NA. Furthermore, N(G)-Nitro-L-arginine methyl amide, which is an isosteric analogue of L-NAME that is much less susceptible to hydrolysis, was a rapidly reversible weak inhibitor of NOS. These data suggested that L-NAME itself was a weak and rapidly reversible inhibitor of nNOS. Most of the inhibition of nNOS by a solution of L-NAME is the result of the formation of L-NA. L-NAME was a substrate for porcine liver esterase.
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