| pubmed-article:566556 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C0042878 | lld:lifeskim |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:566556 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:566556 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:566556 | pubmed:dateCreated | 1978-9-15 | lld:pubmed |
| pubmed-article:566556 | pubmed:abstractText | The membrane-binding characteristics of six vitamin K dependent plasma proteins, which have homologous amino acid sequences, were compared. All of these proteins display calcium-dependent membrane binding and the identified equilibria for protein-membrane binding are qualitatively the same for all proteins. Quantitative characteristics of these protein-membrane interactions allow organization into distinct subgroups. Protein C and factor VII form a subgroup which has extemely low affinity for bilayer membranes; prothrombin, factor X, and protein S form the tightest complexes with membranes and factor IX displays intermediate affinity. In the presence of manganese (which substitutes for calcium in a cation-dependent protein transition), calcium titration of protein-membrane binding shows the same calcium dependence for all proteins except prothrombin which requires lower calcium. These protein-membrane binding characteristics agree very well with the relatedness of these proteins based on their partial amino-terminal sequences. | lld:pubmed |
| pubmed-article:566556 | pubmed:language | eng | lld:pubmed |
| pubmed-article:566556 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:566556 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:566556 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:566556 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:566556 | pubmed:month | May | lld:pubmed |
| pubmed-article:566556 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:566556 | pubmed:author | pubmed-author:KisielWW | lld:pubmed |
| pubmed-article:566556 | pubmed:author | pubmed-author:NelsestuenG... | lld:pubmed |
| pubmed-article:566556 | pubmed:author | pubmed-author:Di ScipioR... | lld:pubmed |
| pubmed-article:566556 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:566556 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:566556 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:566556 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:566556 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:566556 | pubmed:pagination | 2134-8 | lld:pubmed |
| pubmed-article:566556 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:566556 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:566556 | pubmed:articleTitle | Interaction of vitamin K dependent proteins with membranes. | lld:pubmed |
| pubmed-article:566556 | pubmed:publicationType | Journal Article | lld:pubmed |
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