pubmed-article:293717 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C1179841 | lld:lifeskim |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
pubmed-article:293717 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
pubmed-article:293717 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:293717 | pubmed:dateCreated | 1980-3-27 | lld:pubmed |
pubmed-article:293717 | pubmed:abstractText | The distribution of plasma membrane-associated proteins was studied by using latex-filled phagolysosomes prepared from cultured mouse L-929 cells as a model of "inside-out" membrane. Proteins from 131I/lactoperoxidase-labeled phagolysosomes, phagolysosomes derived from 131I/lactoperoxidase-labeled cells, and phagolysosomes prepared from [35S]methionine metabolically labeled cells were analyzed by high-resolution two-dimensional gel electrophoresis. The gel patterns of iodinated proteins showed specific differences in the availability of membrane proteins to lactoperoxidase labeling between inside-out and right-side-out membranes. However, at least two prominent [35S]methionine-labeled proteins of approximately 60,000 and 100,000 daltons were available for iodination at both sides of the membrane. Partial proteolysis of the 100,000-dalton protein revealed that different peptides were iodinated when the iodination was performed on intact cells or on phagolysosomes, consisent with the idea that this protein spans the plasma membrane. | lld:pubmed |
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pubmed-article:293717 | pubmed:language | eng | lld:pubmed |
pubmed-article:293717 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:293717 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:293717 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:293717 | pubmed:month | Dec | lld:pubmed |
pubmed-article:293717 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:293717 | pubmed:author | pubmed-author:FinkL MLM | lld:pubmed |
pubmed-article:293717 | pubmed:author | pubmed-author:WardD CDC | lld:pubmed |
pubmed-article:293717 | pubmed:author | pubmed-author:EvansR MRM | lld:pubmed |
pubmed-article:293717 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:293717 | pubmed:volume | 76 | lld:pubmed |
pubmed-article:293717 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:293717 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:293717 | pubmed:pagination | 6235-9 | lld:pubmed |
pubmed-article:293717 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:293717 | pubmed:year | 1979 | lld:pubmed |
pubmed-article:293717 | pubmed:articleTitle | Asymmetric distribution of plasma membrane proteins in mouse L-929 cells. | lld:pubmed |
pubmed-article:293717 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:293717 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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