pubmed-article:807156 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:807156 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
pubmed-article:807156 | lifeskim:mentions | umls-concept:C2265036 | lld:lifeskim |
pubmed-article:807156 | lifeskim:mentions | umls-concept:C0070368 | lld:lifeskim |
pubmed-article:807156 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:807156 | pubmed:dateCreated | 1975-10-11 | lld:pubmed |
pubmed-article:807156 | pubmed:abstractText | Peptidoglycan transpeptidase and dd-carboxypeptidase have been detected in isolated membranes of Pseudomonas aeruginosa. Cephalosporins and penicillins fail to inhibit the transpeptidase at concentrations as high as 100 mug/ml. dd-Carboxypeptidase, on the other hand, is sensitive to inhibition by beta-lactam antibiotics. The presence of dimethyl sulfoxide in the reaction mixture results in a twofold stimulation of peptidoglycan formation, whereas dd-carboxypeptidase is inhibited approximately 30%. Maximum stimulation of transpeptidase occurs in the presence of both dimethyl sulfoxide and a beta-lactum antibiotic. This is in sharp contrast to the transpeptidase from Escherichia coli, which is sensitive to inhibition by penicillins and cephalosporins. | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:807156 | pubmed:language | eng | lld:pubmed |
pubmed-article:807156 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:807156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:807156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:807156 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:807156 | pubmed:month | May | lld:pubmed |
pubmed-article:807156 | pubmed:issn | 0066-4804 | lld:pubmed |
pubmed-article:807156 | pubmed:author | pubmed-author:RaoV GVG | lld:pubmed |
pubmed-article:807156 | pubmed:author | pubmed-author:PresslitzJ... | lld:pubmed |
pubmed-article:807156 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:807156 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:807156 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:807156 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:807156 | pubmed:pagination | 578-81 | lld:pubmed |
pubmed-article:807156 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-P... | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-C... | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-A... | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-D... | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-P... | lld:pubmed |
pubmed-article:807156 | pubmed:meshHeading | pubmed-meshheading:807156-P... | lld:pubmed |
pubmed-article:807156 | pubmed:year | 1975 | lld:pubmed |
pubmed-article:807156 | pubmed:articleTitle | DD-carboxypeptidase and peptidoglycan transpeptidase from Pseudomonas aeruginosa. | lld:pubmed |
pubmed-article:807156 | pubmed:publicationType | Journal Article | lld:pubmed |
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