pubmed-article:7814395 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0038411 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:7814395 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:7814395 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7814395 | pubmed:dateCreated | 1995-2-3 | lld:pubmed |
pubmed-article:7814395 | pubmed:abstractText | In this report we have analyzed the binding of collagen to Streptococcus pyogenes strain 6414. This binding was rapid, specific, and involved a limited number of receptor molecules (11,600 copies per cell). When the proteins in a streptococcal lysate were blotted onto a nitrocellulose filter and probed with 125I-labeled collagen, a prominent collagen-binding protein of 57 kDa was identified as well as minor 130-150-kDa components. The major 57-kDa protein was isolated by affinity chromatography on collagen-Sepharose followed by gel filtration chromatography. The 57-kDa protein purified from S. pyogenes was used to raise a monospecific antibody which also reacted with a collagen-binding protein of similar molecular size isolated from Streptococcus zooepidemicus. The two collagen-binding proteins from streptococci have a similar amino acid composition and isoelectric points. Isolated collagen-binding protein was specifically recognized by 125I-collagen in a solid-phase binding assay and displayed an affinity for the ligand quite similar to that exhibited by intact bacteria (Kd = 3.1 versus 3.5 x 10(-9) M, respectively). Surface-labeled bacteria attached to microtiter wells coated with different collagen types and the 57-kDa protein blocked the adhesion to collagen substrate. We propose that the 57-kDa protein is an adhesin involved in the attachment of streptococci to host tissues. | lld:pubmed |
pubmed-article:7814395 | pubmed:language | eng | lld:pubmed |
pubmed-article:7814395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7814395 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7814395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7814395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7814395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7814395 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7814395 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7814395 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7814395 | pubmed:author | pubmed-author:SpezialePP | lld:pubmed |
pubmed-article:7814395 | pubmed:author | pubmed-author:TonioloAA | lld:pubmed |
pubmed-article:7814395 | pubmed:author | pubmed-author:RaucciGG | lld:pubmed |
pubmed-article:7814395 | pubmed:author | pubmed-author:BozziniSS | lld:pubmed |
pubmed-article:7814395 | pubmed:author | pubmed-author:VisaiLL | lld:pubmed |
pubmed-article:7814395 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7814395 | pubmed:day | 6 | lld:pubmed |
pubmed-article:7814395 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7814395 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7814395 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7814395 | pubmed:pagination | 347-53 | lld:pubmed |
pubmed-article:7814395 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:7814395 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7814395 | pubmed:articleTitle | Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414. | lld:pubmed |
pubmed-article:7814395 | pubmed:affiliation | Department of Biochemistry, University of Pavia, Italy. | lld:pubmed |
pubmed-article:7814395 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7814395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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