Y. Komori et al., INHIBITION OF PURIFIED NITRIC-OXIDE SYNTHASE FROM RAT CEREBELLUM AND MACROPHAGE BY L-ARGININE ANALOGS, Archives of biochemistry and biophysics, 315(2), 1994, pp. 213-218
The inhibition of nitric oxide synthase (NOS) activity by a variety of
L-arginine-related compounds has been investigated. The inhibitory pr
operties of N-G-amino-, N-G-methyl-, N-G-hydroxy-, N-G-ethyl-, N-G-all
yl-, N-G,N-G-dimethyl-, N-G-methoxy-L-arginine, and several other L-ar
ginine derivatives were compared in NOS purified from both macrophage
and rat cerebellum, Also, these compounds were tested for their potent
ial as alternate substrates by determining their ability to elicit NAD
PH consumption by NOS. N-G-Methoxy-L-arginine appears to be an alterna
te substrate for NOS, whereas most other L-arginine analogs, except fo
r the biosynthetic intermediate N-G-hydroxy-L-arginine, do not elicit
significant enzyme turnover. (C) 1994 Academic Press, Inc.