| pubmed-article:3691660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0024109 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0999699 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0023542 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:3691660 | lifeskim:mentions | umls-concept:C1707520 | lld:lifeskim |
| pubmed-article:3691660 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3691660 | pubmed:dateCreated | 1988-2-8 | lld:pubmed |
| pubmed-article:3691660 | pubmed:abstractText | High affinity binding sites for [3H]leukotriene C4 ([3H]LTC4) have been identified and characterised in guinea-pig lung membranes. [3H]LTC4 bound to these membranes with a pharmacological specificity totally distinct to that previously observed for [3H]LTD4 binding in guinea-pig lung. Scatchard analysis of saturation binding data showed a single class of binding sites, with a dissociation constant (KD) of 52.6 +/- 4.9 nM and a density (Bmax) of 30 +/- 12 pmol/mg membrane protein. The binding was inhibited with high affinity by a variety of glutathione-containing leukotriene analogues. Most notable was the inhibition by 1,2,3,4-tetranor LTC4 (Ki = 118 nM) and S-decylglutathione (Ki = 154 nM) since neither of these compounds were contractile agonists on guinea-pig parenchymal strips or guinea-pig ileum nor were they antagonists of LTC4-induced contractions of these smooth muscle preparations. These results indicate that the observed binding of [3H]LTC4 to guinea-pig lung membranes is not to a contractile receptor. | lld:pubmed |
| pubmed-article:3691660 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3691660 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3691660 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3691660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3691660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3691660 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3691660 | pubmed:issn | 0014-2999 | lld:pubmed |
| pubmed-article:3691660 | pubmed:author | pubmed-author:CuthbertN JNJ | lld:pubmed |
| pubmed-article:3691660 | pubmed:author | pubmed-author:GardinerP JPJ | lld:pubmed |
| pubmed-article:3691660 | pubmed:author | pubmed-author:NormanPP | lld:pubmed |
| pubmed-article:3691660 | pubmed:author | pubmed-author:KluenderH CHC | lld:pubmed |
| pubmed-article:3691660 | pubmed:author | pubmed-author:AbramT STS | lld:pubmed |
| pubmed-article:3691660 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3691660 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:3691660 | pubmed:volume | 143 | lld:pubmed |
| pubmed-article:3691660 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3691660 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3691660 | pubmed:pagination | 323-34 | lld:pubmed |
| pubmed-article:3691660 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:meshHeading | pubmed-meshheading:3691660-... | lld:pubmed |
| pubmed-article:3691660 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3691660 | pubmed:articleTitle | The binding of [3H]leukotriene C4 to guinea-pig lung membranes. The lack of correlation of LTC4 functional activity with binding affinity. | lld:pubmed |
| pubmed-article:3691660 | pubmed:affiliation | Miles Laboratories Ltd., Stoke Poges, Slough, U.K. | lld:pubmed |
| pubmed-article:3691660 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3691660 | pubmed:publicationType | In Vitro | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3691660 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3691660 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3691660 | lld:pubmed |
