| pubmed-article:8503864 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C0015502 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C0040048 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8503864 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:8503864 | pubmed:dateCreated | 1993-6-25 | lld:pubmed |
| pubmed-article:8503864 | pubmed:abstractText | Tissue Factor (TF) is the cellular receptor for coagulation Factor VII/VIIa (FVII/VIIa). TF binds to FVIIa and promotes the rapid activation of the zymogen substrates Factors IX and X (FIX and FX) to the respective serine proteinases. In order to probe structure-function relationships in TF, we have subjected the truncated membrane-bound variant, TF 1-243, to proteolytic digestion in SDS-containing gels. Three major polypeptide fragments were generated by proteolysis of TF 1-243 with chymotrypsin, producing cleavages C-terminal to residues 34, 76 and 103. All three polypeptides, TF 35-243, 77-243 and 104-243, bound biotinylated human FVII in a highly specific ligand blot assay. High-performance electrophoretic chromatography was used to isolated chymotrypsin-derived fragments of TF. These purified fragments bound FVII in ligand blots, and two of the three polypeptides exhibited much reduced, but significant, procoagulant activity in a chromogenic assay for the generation of Factor Xa in the presence of FVIIa and Ca2+. The smallest chymotrypsin-derived TF polypeptide, TF 104-243, showed reduced binding of FVII in ligand blot analyses, inhibited the activity of the full-length molecule, but had no procoagulant activity. These data suggest that a part of the binding site for FVII is contained within the TF sequence 104-243. The sequence TF 1-34 either contains a part of the FVII-binding domain or its removal leads to dysfunctional folding, disrupting binding sites elsewhere in the molecule. | lld:pubmed |
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| pubmed-article:8503864 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8503864 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8503864 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8503864 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8503864 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8503864 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8503864 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8503864 | pubmed:month | May | lld:pubmed |
| pubmed-article:8503864 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8503864 | pubmed:author | pubmed-author:MartinD MDM | lld:pubmed |
| pubmed-article:8503864 | pubmed:author | pubmed-author:ByfieldP GPG | lld:pubmed |
| pubmed-article:8503864 | pubmed:author | pubmed-author:TuddenhamE... | lld:pubmed |
| pubmed-article:8503864 | pubmed:author | pubmed-author:O'BrienD PDP | lld:pubmed |
| pubmed-article:8503864 | pubmed:author | pubmed-author:AndersonJ SJS | lld:pubmed |
| pubmed-article:8503864 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8503864 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8503864 | pubmed:volume | 292 ( Pt 1) | lld:pubmed |
| pubmed-article:8503864 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8503864 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8503864 | pubmed:pagination | 7-12 | lld:pubmed |
| pubmed-article:8503864 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8503864 | pubmed:meshHeading | pubmed-meshheading:8503864-... | lld:pubmed |
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| pubmed-article:8503864 | pubmed:meshHeading | pubmed-meshheading:8503864-... | lld:pubmed |
| pubmed-article:8503864 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8503864 | pubmed:articleTitle | Structural requirements for the interaction between tissue factor and factor VII: characterization of chymotrypsin-derived tissue factor polypeptides. | lld:pubmed |
| pubmed-article:8503864 | pubmed:affiliation | Haemostasis Research Group, Clinical Research Centre, Harrow, Middx., U.K. | lld:pubmed |
| pubmed-article:8503864 | pubmed:publicationType | Journal Article | lld:pubmed |
