pubmed-article:7354047 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0054961 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C1335285 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0883208 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0743223 | lld:lifeskim |
pubmed-article:7354047 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
pubmed-article:7354047 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:7354047 | pubmed:dateCreated | 1980-4-23 | lld:pubmed |
pubmed-article:7354047 | pubmed:abstractText | T200 glycoprotein, a major cell surface component of murine hematopoietic cells, is a phosphorylated transmembrane glycoprotein. Two distinct regions of the molecule can be defined by radiolabeling with a variety of metabolic precursors or by lactoperoxidase-catalyzed iodination, in combination with protease treatments, immunoprecipitation techniques, and peptide "mapping" analysis. A relative protease-resistant domain, which is exposed on the cell surface and contains the antigenic site recognized by a monoclonal anti-T200 antibody known to react with the exterior cell surface, contains most if not all of the mannose-containing oligosaccharide units of the glycoprotein and all of the amino acid residues labeled by lactoperoxidase-catalyzed iodination of intact viable cells. This protease-resistant fragment migrates with an apparent molecular weight of approximately 100,000 in sodium dodecyl sulfate-polyacrylamide gels. The remaining portion of the molecule contains a region, extensively digested by trypsin, which is exposed on the cytoplasmic side of the plasma membrane and contains phosphoserine residues which can be labeled with 32PO4 in vivo. A 125I-labeled tryptic peptide derived from this region of the molecule was obtained if membrane preparations from cells disrupted by nitrogen cavitation were labeled by lactoperoxidase-catalyzed iodination. | lld:pubmed |
pubmed-article:7354047 | pubmed:language | eng | lld:pubmed |
pubmed-article:7354047 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7354047 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7354047 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7354047 | pubmed:month | Feb | lld:pubmed |
pubmed-article:7354047 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7354047 | pubmed:author | pubmed-author:TrowbridgeI... | lld:pubmed |
pubmed-article:7354047 | pubmed:author | pubmed-author:PRATTC WCW | lld:pubmed |
pubmed-article:7354047 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7354047 | pubmed:day | 25 | lld:pubmed |
pubmed-article:7354047 | pubmed:volume | 255 | lld:pubmed |
pubmed-article:7354047 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7354047 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7354047 | pubmed:pagination | 1662-9 | lld:pubmed |
pubmed-article:7354047 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:7354047 | pubmed:meshHeading | pubmed-meshheading:7354047-... | lld:pubmed |
pubmed-article:7354047 | pubmed:year | 1980 | lld:pubmed |
pubmed-article:7354047 | pubmed:articleTitle | Disposition of T200 glycoprotein in the plasma membrane of a murine lymphoma cell line. | lld:pubmed |
pubmed-article:7354047 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7354047 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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