| pubmed-article:6238974 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C0003250 | lld:lifeskim |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:6238974 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:6238974 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:6238974 | pubmed:dateCreated | 1985-1-17 | lld:pubmed |
| pubmed-article:6238974 | pubmed:abstractText | To identify platelet surface structures involved in adhesion to collagen, the effect of 16 murine antiplatelet membrane hybridoma antibodies were tested in a defined, in vitro assay. Four of these antibodies inhibited platelet-collagen adhesion and reacted with a polypeptide with Mr approximately 125,000, as determined by immunoblots after gel electrophoresis under reducing conditions. Through detailed studies with one of these antibodies, the monoclonal antibody PMI-1, the relevant antigen was identified as platelet glycoprotein IIb alpha, based upon (a) co-migration with this glycoprotein in two-dimensional gel electrophoresis and (b) co-purification by immunoaffinity chromatography with a protein with apparent Mr identical to that of glycoprotein III, under conditions in which glycoproteins IIb and III form a complex. Univalent antibody fragments prepared from monoclonal antibody PMI-1 inhibited greater than 80% of platelet-collagen adhesion, and inhibition was completely blocked by the immunopurified antigen. These results indicate that glycoprotein IIb participates in some aspect of platelet-collagen adhesion. In contrast, the purified antigen only partially neutralized a polyclonal antiserum that blocked platelet-collagen adhesion, to a maximum of approximately 25%, at saturating antigen concentrations. Thus, by these immunological criteria, glycoprotein IIb is not the only molecule involved in this process. | lld:pubmed |
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| pubmed-article:6238974 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6238974 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6238974 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6238974 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6238974 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:6238974 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:6238974 | pubmed:author | pubmed-author:BarondesS HSH | lld:pubmed |
| pubmed-article:6238974 | pubmed:author | pubmed-author:PlowE FEF | lld:pubmed |
| pubmed-article:6238974 | pubmed:author | pubmed-author:GinsbergM HMH | lld:pubmed |
| pubmed-article:6238974 | pubmed:author | pubmed-author:ShadleP JPJ | lld:pubmed |
| pubmed-article:6238974 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6238974 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:6238974 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6238974 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6238974 | pubmed:pagination | 2056-60 | lld:pubmed |
| pubmed-article:6238974 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6238974 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6238974 | pubmed:articleTitle | Platelet-collagen adhesion: inhibition by a monoclonal antibody that binds glycoprotein IIb. | lld:pubmed |
| pubmed-article:6238974 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6238974 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6238974 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:6238974 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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