| pubmed-article:2390065 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:2390065 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2390065 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2390065 | pubmed:dateCreated | 1990-9-25 | lld:pubmed |
| pubmed-article:2390065 | pubmed:abstractText | We describe the isolation, lipid-binding properties and partial amino acid sequence of PS-p68, a novel 68 kDa phosphatidylserine-binding protein from human platelets. PS-p68 is an abundant constituent of platelets, accounting for 0.5-0.75% of total cell protein. It was purified from platelet cytosol by affinity chromatography. Amino acid sequence analysis yielded no similarity to identified proteins. In contrast with most known phospholipid-binding proteins, PS-p68 does not bind Ca2+ and does not require Ca2+ for its binding of phosphatidylserine. Phosphatidylserine binding to PS-p68 was inhibited by phosphatidic acid and by alkylphospholipids. PS-p68 was isolated as a major phosphoprotein from 32P-labelled platelets and was found to function as a protein kinase C substrate in vitro. However, treatment of intact platelets with phorbol 12-myristate 13-acetate, thrombin or carbacyclin did not increase PS-p68 phosphorylation. Platelets appear to be the only blood cells containing PS-p68, which was not detected in neutrophils, monocytes and lymphocytes. | lld:pubmed |
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| pubmed-article:2390065 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2390065 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2390065 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2390065 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2390065 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2390065 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2390065 | pubmed:author | pubmed-author:BaggioliniMM | lld:pubmed |
| pubmed-article:2390065 | pubmed:author | pubmed-author:WolfMM | lld:pubmed |
| pubmed-article:2390065 | pubmed:author | pubmed-author:GanzTT | lld:pubmed |
| pubmed-article:2390065 | pubmed:author | pubmed-author:BurgenerRR | lld:pubmed |
| pubmed-article:2390065 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2390065 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2390065 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:2390065 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2390065 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2390065 | pubmed:pagination | 729-34 | lld:pubmed |
| pubmed-article:2390065 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2390065 | pubmed:meshHeading | pubmed-meshheading:2390065-... | lld:pubmed |
| pubmed-article:2390065 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2390065 | pubmed:articleTitle | Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets. | lld:pubmed |
| pubmed-article:2390065 | pubmed:affiliation | Theodor Kocher Institut, Universität Bern, Switzerland. | lld:pubmed |
| pubmed-article:2390065 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:8436 | entrezgene:pubmed | pubmed-article:2390065 | lld:entrezgene |
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