| pubmed-article:2557328 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2557328 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2557328 | lifeskim:mentions | umls-concept:C0039259 | lld:lifeskim |
| pubmed-article:2557328 | lifeskim:mentions | umls-concept:C0061688 | lld:lifeskim |
| pubmed-article:2557328 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:2557328 | lifeskim:mentions | umls-concept:C1149539 | lld:lifeskim |
| pubmed-article:2557328 | pubmed:issue | 36 | lld:pubmed |
| pubmed-article:2557328 | pubmed:dateCreated | 1990-2-1 | lld:pubmed |
| pubmed-article:2557328 | pubmed:abstractText | Membrane-associated and soluble forms of folate binding protein (FBP) have been identified in mammalian tissues and biological fluids. Despite their solubility differences, these two forms are functionally similar, immunologically cross-reacting, and have the same apparent molecular weights. In this study we demonstrate, for the first time, that the membrane FBP of cultured human KB cells contains a glycosyl-phosphatidylinositol (GPI) tail which is responsible for its hydrophobic properties and distinguishes it from the soluble FBP released into the medium. Treatment of the purified membrane FBP with phospholipase C specific for phosphatidylinositol (PI-PLC) removed the GPI tail and converted it to the soluble form without a change in apparent Mr by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In addition, virtually all of the folate binding sites on the plasma membrane of the intact cells were released as soluble, functional FBP following treatment with PI-PLC. The GPI tail contained 1-O-alkyl-2-O-acylglycerol as a mixture of fatty alcohols in ether linkage at C1 of the glycerol backbone and almost exclusively docosanoic acid (22:0) as the fatty acid on C2. The inositol also contained a mixture of fatty acids (16:0, 18:0, 18:1, 20:4, 22:0) located on a site other than the C2 position since the FBP was susceptible to PI-PLC cleavage. After nitrous acid deamination, the aqueous portion of the FBP contained covalently bound fatty acids, predominantly palmitate (16:0) and stearate (18:0), indicating the presence of additional acyl groups attached to the peptide in the form of amide, ester, or thioester linkage. | lld:pubmed |
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| pubmed-article:2557328 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2557328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557328 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2557328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2557328 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2557328 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2557328 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2557328 | pubmed:author | pubmed-author:SlomianyB LBL | lld:pubmed |
| pubmed-article:2557328 | pubmed:author | pubmed-author:LuhrsC ACA | lld:pubmed |
| pubmed-article:2557328 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2557328 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:2557328 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2557328 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2557328 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2557328 | pubmed:pagination | 21446-9 | lld:pubmed |
| pubmed-article:2557328 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:2557328 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2557328 | pubmed:articleTitle | A human membrane-associated folate binding protein is anchored by a glycosyl-phosphatidylinositol tail. | lld:pubmed |
| pubmed-article:2557328 | pubmed:affiliation | Department of Medicine, State University of New York-Health Science Center, Brooklyn. | lld:pubmed |
| pubmed-article:2557328 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2557328 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2557328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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