| pubmed-article:3755431 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3755431 | lifeskim:mentions | umls-concept:C0015498 | lld:lifeskim |
| pubmed-article:3755431 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3755431 | lifeskim:mentions | umls-concept:C0483249 | lld:lifeskim |
| pubmed-article:3755431 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:3755431 | pubmed:dateCreated | 1986-9-17 | lld:pubmed |
| pubmed-article:3755431 | pubmed:abstractText | Activated protein C has been derivatized with the active site-directed fluorophore 2-(dimethylamino)-6-naphthalenesulfonylglutamylglycylarginyl chloromethyl ketone (2,6-DEGR-APC). Covalently modified activated protein C has been used to investigate the binding interactions of the protein to factors V and Va in the presence of phospholipid vesicles. The fluorescence polarization of the 6-dimethylaminonaphthalene-2-sulfonyl moiety increased saturably with increasing phospholipid concentrations in the presence or absence of factor V or Va. Differences in the limiting polarization values indicated distinguishable differences in the interactions between 2,6-DEGR-APC and phospholipid in the presence of factor V or Va. The dissociation constant calculated for the 2,6-DEGR-APC/phospholipid interaction (7.3 X 10(-8) M) was not significantly altered by factor V but was decreased to 7 X 10(-9) M in the presence of factor Va. The interaction between 2,6-DEGR-APC and factor V or Va was characterized by a 1:1 stoichiometry. The binding of 2,6-DEGR-APC to factor V or Va in the presence of phospholipid could be reduced in a competitive manner by diisopropylphosphofluoridate-treated activated protein C. An analysis of the displacement curves indicated that the binding of 2,6-DEGR-APC was indistinguishable from the binding of diisopropylphosphofluoridate-treated activated protein C. The interaction between 2,6-DEGR-APC and phospholipid-bound factor Va was further examined using the isolated subunits of factor Va. Fluorescence polarization changes observed with component E of Va (light chain) closely corresponded with the changes observed with factor Va, whereas isolated component D (heavy chain) had little influence on the binding of 2,6-DEGR-APC to phospholipid vesicles. The data presented are consistent with the interpretation that component E of factor Va contains a binding site for activated protein C. | lld:pubmed |
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| pubmed-article:3755431 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3755431 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3755431 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3755431 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3755431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3755431 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3755431 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3755431 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3755431 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3755431 | pubmed:author | pubmed-author:MannK GKG | lld:pubmed |
| pubmed-article:3755431 | pubmed:author | pubmed-author:WilliamsE BEB | lld:pubmed |
| pubmed-article:3755431 | pubmed:author | pubmed-author:KrishnaswamyS... | lld:pubmed |
| pubmed-article:3755431 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3755431 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:3755431 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:3755431 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3755431 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3755431 | pubmed:pagination | 9684-93 | lld:pubmed |
| pubmed-article:3755431 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:3755431 | pubmed:meshHeading | pubmed-meshheading:3755431-... | lld:pubmed |
| pubmed-article:3755431 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3755431 | pubmed:articleTitle | The binding of activated protein C to factors V and Va. | lld:pubmed |
| pubmed-article:3755431 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3755431 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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