| pubmed-article:16789148 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0004651 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:16789148 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:16789148 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16789148 | pubmed:dateCreated | 2010-6-29 | lld:pubmed |
| pubmed-article:16789148 | pubmed:abstractText | Under most conditions of growth, the most abundant protein in the outer membrane of most strains of Escherichia coli is a protein designated as "protein 1" or "matrix protein". In E. coli B, this protein has been shown to be a single polypeptide with a molecular mass of 36,500 and it may account for more than 50% of the total outer membrane protein. E. coli K-12 contains a very similar, although probably not identical, species of protein 1. Some pathogenic E. coli strains contain very little protein 1 and, in its place, make a protein designated as protein 2 which migrates faster on alkaline polyacrylamide gels containing sodium dodecyl sulfate and which gives a different spectrum of CNBr peptides. An E. coli K-12 strain which had been mated with a pathogenic strain was found to produce protein 2, and a temperate bacteriophage was isolated from this K-12 strain after induction with UV light. This phage, designated as PA-2, is similar in morphology and several other properties to phage lambda. When strains of E. coli K-12 are lysogenized by phage PA-2, they produce protein 2 and very little protein 1. Adsorption to lysogenic strains grown under conditions where they produce little protein 1 and primarily protein 2 is greatly reduced as compared to non-lysogenic strains which produce only protein 1. However, when cultures are grown under conditions of catabolite repression, protein 2 is reduced and protein 1 is increased, and lysogenic and non-lysogenic cultures grown under these conditions exhibit the same rate of adsorption. Phage PA-2 does not adsorb to E. coli B, which appears to have a slightly different protein 1 from K-12. These results suggest that protein 1 is the receptor for PA-2, and that protein 2 is made to reduce the superinfection of lysogens. | lld:pubmed |
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| pubmed-article:16789148 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16789148 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16789148 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:16789148 | pubmed:month | May | lld:pubmed |
| pubmed-article:16789148 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16789148 | pubmed:author | pubmed-author:SmithDD | lld:pubmed |
| pubmed-article:16789148 | pubmed:author | pubmed-author:SchnaitmanCC | lld:pubmed |
| pubmed-article:16789148 | pubmed:author | pubmed-author:de SalsasM... | lld:pubmed |
| pubmed-article:16789148 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16789148 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:16789148 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16789148 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16789148 | pubmed:pagination | 1121-30 | lld:pubmed |
| pubmed-article:16789148 | pubmed:dateRevised | 2010-9-15 | lld:pubmed |
| pubmed-article:16789148 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:16789148 | pubmed:articleTitle | Temperate Bacteriophage Which Causes the Production of a New Major Outer Membrane Protein by Escherichia coli. | lld:pubmed |
| pubmed-article:16789148 | pubmed:affiliation | Department of Microbiology, The University of Virginia, Charlottesville, Virginia 22901. | lld:pubmed |
| pubmed-article:16789148 | pubmed:publicationType | Journal Article | lld:pubmed |
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