pubmed-article:836823 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0025248 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0023206 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:836823 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
pubmed-article:836823 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:836823 | pubmed:dateCreated | 1977-4-28 | lld:pubmed |
pubmed-article:836823 | pubmed:abstractText | The major platelet membrane glycoproteins have been solubilized in 1.0% sodium deoxycholate and subjected to affinity chromatography on the lectins from Lens culinaris, wheat germ and Abrus precatorius. Polyacrylamide gel electrophoresis in the presence and absence of a reducing agent together with the differential binding of the lectins to the glycoproteins permitted the distinction of at least seven separate glycoprotein entities. A new nomenclature for the glycoproteins is proposed to accomodate the additional data. Using combinations of lectin columns, glycoproteins Ia and Ib could be prepared in a pure state and IIb and IIIa could be greatly purified. The binding of lectins to glycoprotein Ib has been strongly implicated as a necessary step in the aggregation response of platelets to lectins. | lld:pubmed |
pubmed-article:836823 | pubmed:language | eng | lld:pubmed |
pubmed-article:836823 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:836823 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:836823 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:836823 | pubmed:month | Feb | lld:pubmed |
pubmed-article:836823 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:836823 | pubmed:author | pubmed-author:JenkinsC SCS | lld:pubmed |
pubmed-article:836823 | pubmed:author | pubmed-author:ClemetsonK... | lld:pubmed |
pubmed-article:836823 | pubmed:author | pubmed-author:PfuellerS LSL | lld:pubmed |
pubmed-article:836823 | pubmed:author | pubmed-author:LuscherE FEF | lld:pubmed |
pubmed-article:836823 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:836823 | pubmed:day | 4 | lld:pubmed |
pubmed-article:836823 | pubmed:volume | 464 | lld:pubmed |
pubmed-article:836823 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:836823 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:836823 | pubmed:pagination | 493-508 | lld:pubmed |
pubmed-article:836823 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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pubmed-article:836823 | pubmed:meshHeading | pubmed-meshheading:836823-C... | lld:pubmed |
pubmed-article:836823 | pubmed:year | 1977 | lld:pubmed |
pubmed-article:836823 | pubmed:articleTitle | Isolation of the membrane glycoproteins of human blood platelets by lectin affinity chromatography. | lld:pubmed |
pubmed-article:836823 | pubmed:publicationType | Journal Article | lld:pubmed |
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