pubmed-article:3980079 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3980079 | lifeskim:mentions | umls-concept:C0023237 | lld:lifeskim |
pubmed-article:3980079 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
pubmed-article:3980079 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
pubmed-article:3980079 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3980079 | pubmed:dateCreated | 1985-5-15 | lld:pubmed |
pubmed-article:3980079 | pubmed:abstractText | Legionella pneumophila and related species were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis for outer membrane proteins. Of the 10 species examined, 9 contained a 24-kilodalton (kDa) major outer membrane protein (MOMP) that was resolvable only when outer membrane material was heated in the presence of 2-mercaptoethanol. Labeling studies with [35S]cysteine indicated that the protein contained cysteine, and disulfide cross-linking of the unreduced complex was demonstrated by labeling with iodoacetamide. The unreduced outer membrane preparation contained peptidoglycan, and after treatment with lysozyme to remove peptidoglycan, a protein complex of 95 kDa was observed by sodium dodecyl sulfate polyacrylamide gel electrophoresis in the absence of 2-mercaptoethanol. Reduction of the 95-kDa complex yielded 24-kDa monomers, suggesting that the 95-kDa complex was composed of four subunits. The 24-kDa MOMP from L. pneumophila was purified, and antibody produced to this protein cross-reacted with all species of Legionella as determined from an immunoblot of a sodium dodecyl sulfate gel. Only serogroup 1 strains of L. bozemanii lacked the 24-kDa MOMP and showed no cross-reactivity. These results suggest that the 24-kDa MOMP common to most species of Legionella contains a genus-specific epitope. | lld:pubmed |
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pubmed-article:3980079 | pubmed:language | eng | lld:pubmed |
pubmed-article:3980079 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3980079 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3980079 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3980079 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3980079 | pubmed:issn | 0019-9567 | lld:pubmed |
pubmed-article:3980079 | pubmed:author | pubmed-author:HoffmanP SPS | lld:pubmed |
pubmed-article:3980079 | pubmed:author | pubmed-author:HatchT PTP | lld:pubmed |
pubmed-article:3980079 | pubmed:author | pubmed-author:ButlerC ACA | lld:pubmed |
pubmed-article:3980079 | pubmed:author | pubmed-author:StreetE DED | lld:pubmed |
pubmed-article:3980079 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3980079 | pubmed:volume | 48 | lld:pubmed |
pubmed-article:3980079 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3980079 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3980079 | pubmed:pagination | 14-8 | lld:pubmed |
pubmed-article:3980079 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:3980079 | pubmed:meshHeading | pubmed-meshheading:3980079-... | lld:pubmed |
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pubmed-article:3980079 | pubmed:meshHeading | pubmed-meshheading:3980079-... | lld:pubmed |
pubmed-article:3980079 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:3980079 | pubmed:articleTitle | Disulfide-bonded outer membrane proteins in the genus Legionella. | lld:pubmed |
pubmed-article:3980079 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3980079 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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