当前位置： SCI文献检索 > LIFE SCIENCES期刊下所有文献 > Potent inhibition of human neuronal nitric oxide synthase by N(G)-nitro-L-arginine methyl ester results from contaminating N(G)-nitro-L-arginine.

Potent inhibition of human neuronal nitric oxide synthase by N(G)-nitro-L-arginine methyl ester results from contaminating N(G)-nitro-L-arginine.

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.

journal_name

Life Sci

journal_title

Life sciences

authors

Furfine ES,Carbine K,Bunker S,Tanoury G,Harmon M,Laubach V,Sherman P

doi

10.1016/s0024-3205(97)00140-9

subject

Has Abstract

pub_date

1997-01-01 00:00:00

pages

1803-9

issue

20

eissn

0024-3205

issn

1879-0631

pii

S0024320597001409

journal_volume

60

pub_type

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