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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1989-7-18
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-924X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
478-83
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:2543663-Antibodies, Monoclonal,
pubmed-meshheading:2543663-Antigen-Antibody Reactions,
pubmed-meshheading:2543663-Binding, Competitive,
pubmed-meshheading:2543663-Calcium,
pubmed-meshheading:2543663-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2543663-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:2543663-Horseradish Peroxidase,
pubmed-meshheading:2543663-Humans,
pubmed-meshheading:2543663-Immunoblotting,
pubmed-meshheading:2543663-Indicators and Reagents,
pubmed-meshheading:2543663-Iodine Radioisotopes,
pubmed-meshheading:2543663-Protein C,
pubmed-meshheading:2543663-Protein Conformation,
pubmed-meshheading:2543663-Radioimmunoassay,
pubmed-meshheading:2543663-Receptors, Cell Surface,
pubmed-meshheading:2543663-Receptors, Thrombin,
pubmed-meshheading:2543663-Thrombin,
pubmed-meshheading:2543663-Whole Blood Coagulation Time
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pubmed:year |
1989
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pubmed:articleTitle |
Monoclonal antibodies to human thrombomodulin whose binding is calcium dependent.
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pubmed:affiliation |
Tokyo Research Institute, Kowa Ltd.
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pubmed:publicationType |
Journal Article
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