Document Detail

Effect of nitric oxide synthase substrate analog inhibitors on rat liver arginase.
MedLine Citation:
PMID:  7505570     Owner:  NLM     Status:  MEDLINE    
Nitric oxide synthase (EC 1.14.23) substrate analog inhibitors NG-monomethyl-L-Arg, NG-nitro-L-Arg, NG-nitro-L-Arg methyl ester, and aminoguanidine were examined as potential inhibitors of rat liver arginase (EC NG-nitro-L-Arg was found to inhibit arginase catalyzed conversion of L-Arg to L-Orn at pH 7.5 with an IC50 = 27.2 +/- 4.3 mM, compared to L-Val and L-Lys with IC50 values of 6.2 +/- 0.4 mM and 31.3 +/- 2.7 mM, respectively. Inhibition was stereospecific for the L-amino acid, not NG-nitro-D-Arg, and required a free alpha-carboxyl group. NG-nitro-L-Arg was not a substrate for rat liver arginase. These results suggest that arginase inhibition should also be evaluated when studying the effects of NOS substrate analog inhibitors in vivo.
C A Robertson; B G Green; L Niedzwiecki; R K Harrison; S K Grant
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  197     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1993 Dec 
Date Detail:
Created Date:  1994-01-25     Completed Date:  1994-01-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  523-8     Citation Subset:  IM    
Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065.
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MeSH Terms
Amino Acid Oxidoreductases / antagonists & inhibitors,  metabolism*
Arginase / antagonists & inhibitors,  metabolism*
Arginine / analogs & derivatives*,  pharmacology
Liver / enzymology*
NG-Nitroarginine Methyl Ester
Nitric Oxide Synthase
Reg. No./Substance:
17035-90-4/omega-N-Methylarginine; 2149-70-4/Nitroarginine; 50903-99-6/NG-Nitroarginine Methyl Ester; 74-79-3/Arginine; EC Oxide Synthase; EC 1.4.-/Amino Acid Oxidoreductases; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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