| pubmed-article:3183615 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0038172 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0009118 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0009017 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:3183615 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:3183615 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3183615 | pubmed:dateCreated | 1988-12-20 | lld:pubmed |
| pubmed-article:3183615 | pubmed:abstractText | The gene coding for coagulase (coa) was cloned from Staphylococcus aureus 8325-4 in a lambda replacement vector in Escherichia coli. Coagulase (plasma-clotting) activity was measured in lambda coa lysates and an immunoreactive protein of 60 kDa was detected by Western immunoblotting with anti-coagulase serum. This protein comigrated with the major immunoreactive protein in supernatants of S. aureus 8325-4. The coa gene was subcloned in pUC vectors. One recombinant expressed a 60 kDa immunoreactive protein and plasma-clotting activity. A putative beta-galactosidase-coagulase fusion protein and truncated peptides were expressed by variants formed by subcloning. These results are consistent with previously published biochemical data that the prothrombin-binding domain of coagulase is located in the N-terminus of the protein. The cloned coa gene was transferred into S. aureus on a shuttle plasmid. Expression of coagulase was higher in a strain with a mutation in the agr locus, which controls the level of several exoproteins in S. aureus, suggesting that agr normally regulates coagulase expression negatively. | lld:pubmed |
| pubmed-article:3183615 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3183615 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3183615 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3183615 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3183615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3183615 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3183615 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3183615 | pubmed:issn | 0022-1287 | lld:pubmed |
| pubmed-article:3183615 | pubmed:author | pubmed-author:FosterT JTJ | lld:pubmed |
| pubmed-article:3183615 | pubmed:author | pubmed-author:O'ReillyMM | lld:pubmed |
| pubmed-article:3183615 | pubmed:author | pubmed-author:O'TooleP WPW | lld:pubmed |
| pubmed-article:3183615 | pubmed:author | pubmed-author:PhonimdaengPP | lld:pubmed |
| pubmed-article:3183615 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3183615 | pubmed:volume | 134 | lld:pubmed |
| pubmed-article:3183615 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3183615 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3183615 | pubmed:pagination | 75-83 | lld:pubmed |
| pubmed-article:3183615 | pubmed:dateRevised | 2010-8-25 | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:meshHeading | pubmed-meshheading:3183615-... | lld:pubmed |
| pubmed-article:3183615 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3183615 | pubmed:articleTitle | Molecular cloning and expression of the coagulase gene of Staphylococcus aureus 8325-4. | lld:pubmed |
| pubmed-article:3183615 | pubmed:affiliation | Microbiology Department, Moyne Institute, Trinity College, Dublin, Ireland. | lld:pubmed |
| pubmed-article:3183615 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3183615 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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