| pubmed-article:2543663 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:2543663 | lifeskim:mentions | umls-concept:C2744539 | lld:lifeskim |
| pubmed-article:2543663 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2543663 | pubmed:dateCreated | 1989-7-18 | lld:pubmed |
| pubmed-article:2543663 | pubmed:abstractText | Four monoclonal antibodies to human thrombomodulin were characterized. Binding of two of these antibodies was dependent on the presence of calcium ions, and approximately 5 mM calcium was required for their maximum binding. These two antibodies inhibited the binding of thrombin to thrombomodulin, thereby inhibiting activation of protein C catalyzed by thrombin-thrombomodulin complex. These two antibodies bind to a major active fragment formed by limited proteolytic digestions of thrombomodulin with elastase and trypsin, suggesting that the antibodies bind to the thrombin-binding site (or its vicinity) located in the epidermal growth factor (EGF)-homology domain. One of the other calcium-independent antibodies also inhibited the binding of thrombin and the activation of protein C, but the inhibition was very weak and was observed only when the antibody was present in a molar excess over thrombomodulin. This antibody did not bind to the protease digests of thrombomodulin. Another calcium-independent antibody did not inhibit either thrombin binding or protein C activation, but bound to the active fragment of protease digests, suggesting that the antibody binds to a region other than the thrombin-binding site in the EGF-homology domain. These observations suggest that thrombomodulin undergoes a calcium-dependent conformational change which may occur in proximity to a thrombin-binding site located in the EGF-homology domain. | lld:pubmed |
| pubmed-article:2543663 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2543663 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2543663 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2543663 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2543663 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:2543663 | pubmed:author | pubmed-author:KimuraSS | lld:pubmed |
| pubmed-article:2543663 | pubmed:author | pubmed-author:AokiNN | lld:pubmed |
| pubmed-article:2543663 | pubmed:author | pubmed-author:NagoyaTT | lld:pubmed |
| pubmed-article:2543663 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2543663 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:2543663 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2543663 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2543663 | pubmed:pagination | 478-83 | lld:pubmed |
| pubmed-article:2543663 | pubmed:dateRevised | 2007-12-19 | lld:pubmed |
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| pubmed-article:2543663 | pubmed:meshHeading | pubmed-meshheading:2543663-... | lld:pubmed |
| pubmed-article:2543663 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2543663 | pubmed:articleTitle | Monoclonal antibodies to human thrombomodulin whose binding is calcium dependent. | lld:pubmed |
| pubmed-article:2543663 | pubmed:affiliation | Tokyo Research Institute, Kowa Ltd. | lld:pubmed |
| pubmed-article:2543663 | pubmed:publicationType | Journal Article | lld:pubmed |
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