| pubmed-article:2871174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2871174 | lifeskim:mentions | umls-concept:C0006100 | lld:lifeskim |
| pubmed-article:2871174 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:2871174 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:2871174 | lifeskim:mentions | umls-concept:C0439284 | lld:lifeskim |
| pubmed-article:2871174 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2871174 | pubmed:dateCreated | 1986-6-23 | lld:pubmed |
| pubmed-article:2871174 | pubmed:abstractText | Bradykinin (BK) and related peptides exert a wide range of effects on several organ systems. We have attempted to sort out these effects by studying the binding interaction of [3H]BK at the membrane level with in vitro receptor binding techniques. High specific activity [3H]BK and an enzyme inhibitor "cocktail" has enabled us to label two BK binding sites with different affinity and peptide specificity in several guinea-pig tissues. In the guinea-pig ileum the high-affinity site has an equilibrium dissociation constant (Kd) for [3H]BK of 13 pM and a maximal number of binding sites of 8.3 pmol/g of tissue wet weight. The low-affinity guinea-pig ileum site displays a Kd of 910 pM, a maximum number of binding sites of 14 pmol/g of tissue wet weight and shows a greater selectivity for BK analogs over Lysyl-BK analogs. Two similar sites can also be discriminated in kidney and heart. The potencies of a series of BK analogs at the high-affinity guinea-pig ileum site correlate well with their potencies in contracting ileal smooth muscle. The binding of [3H]BK in the guinea-pig ileum is inhibited by physiological concentrations of monovalent and divalent cations. | lld:pubmed |
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| pubmed-article:2871174 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2871174 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2871174 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2871174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2871174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2871174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2871174 | pubmed:month | May | lld:pubmed |
| pubmed-article:2871174 | pubmed:issn | 0022-3565 | lld:pubmed |
| pubmed-article:2871174 | pubmed:author | pubmed-author:StewartJ MJM | lld:pubmed |
| pubmed-article:2871174 | pubmed:author | pubmed-author:SnyderS HSH | lld:pubmed |
| pubmed-article:2871174 | pubmed:author | pubmed-author:ManningD CDC | lld:pubmed |
| pubmed-article:2871174 | pubmed:author | pubmed-author:VavrekRR | lld:pubmed |
| pubmed-article:2871174 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2871174 | pubmed:volume | 237 | lld:pubmed |
| pubmed-article:2871174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2871174 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2871174 | pubmed:pagination | 504-12 | lld:pubmed |
| pubmed-article:2871174 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2871174 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2871174 | pubmed:articleTitle | Two bradykinin binding sites with picomolar affinities. | lld:pubmed |
| pubmed-article:2871174 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2871174 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2871174 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2871174 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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