pubmed-article:7520872 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7520872 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:7520872 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
pubmed-article:7520872 | lifeskim:mentions | umls-concept:C0907533 | lld:lifeskim |
pubmed-article:7520872 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:7520872 | lifeskim:mentions | umls-concept:C0020923 | lld:lifeskim |
pubmed-article:7520872 | pubmed:issue | 2-3 | lld:pubmed |
pubmed-article:7520872 | pubmed:dateCreated | 1994-9-26 | lld:pubmed |
pubmed-article:7520872 | 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. | lld:pubmed |
pubmed-article:7520872 | pubmed:language | eng | lld:pubmed |
pubmed-article:7520872 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7520872 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7520872 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7520872 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:7520872 | pubmed:author | pubmed-author:SchmidtKK | lld:pubmed |
pubmed-article:7520872 | pubmed:author | pubmed-author:MayerBB | lld:pubmed |
pubmed-article:7520872 | pubmed:author | pubmed-author:WernerE RER | lld:pubmed |
pubmed-article:7520872 | pubmed:author | pubmed-author:KlattPP | lld:pubmed |
pubmed-article:7520872 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7520872 | pubmed:day | 22 | lld:pubmed |
pubmed-article:7520872 | pubmed:volume | 350 | lld:pubmed |
pubmed-article:7520872 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7520872 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7520872 | pubmed:pagination | 199-202 | lld:pubmed |
pubmed-article:7520872 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:meshHeading | pubmed-meshheading:7520872-... | lld:pubmed |
pubmed-article:7520872 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7520872 | pubmed:articleTitle | Identification of imidazole as L-arginine-competitive inhibitor of porcine brain nitric oxide synthase. | lld:pubmed |
pubmed-article:7520872 | pubmed:affiliation | Institut für Pharmakologie und Toxikologie, Karl-Franzens-Universität Graz, Austria. | lld:pubmed |
pubmed-article:7520872 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7520872 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:7520872 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7520872 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7520872 | lld:pubmed |