rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2-3
|
pubmed:dateCreated |
1994-9-26
|
pubmed:abstractText |
Imidazole acts as a heme-site inhibitor of nitric oxide synthase (NOS). We used this compound to investigate whether the substrate L-arginine binds directly to the heme or to a separate domain of brain NOS. Enzyme kinetic experiments showed that imidazole enhanced the apparent Km for L-arginine without affecting maximal enzyme activity, and binding studies revealed that the inhibitor displaced the radioligand NG-nitro-L-[3H]arginine in a concentration-dependent fashion. These results demonstrate that imidazole exerts its effects on NOS in an L-arginine-competitive manner and that the substrate site of the enzyme may be identical with the prosthetic heme group.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
22
|
pubmed:volume |
350
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
199-202
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7520872-Amino Acid Oxidoreductases,
pubmed-meshheading:7520872-Animals,
pubmed-meshheading:7520872-Arginine,
pubmed-meshheading:7520872-Binding, Competitive,
pubmed-meshheading:7520872-Binding Sites,
pubmed-meshheading:7520872-Biopterin,
pubmed-meshheading:7520872-Brain,
pubmed-meshheading:7520872-Imidazoles,
pubmed-meshheading:7520872-Nitric Oxide Synthase,
pubmed-meshheading:7520872-Swine
|
pubmed:year |
1994
|
pubmed:articleTitle |
Identification of imidazole as L-arginine-competitive inhibitor of porcine brain nitric oxide synthase.
|
pubmed:affiliation |
Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|