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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1997-2-27
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pubmed:abstractText |
We analyzed the penicillin-binding protein (PBP) profiles of two clinical isolates of Enterococcus faecalis for which ampicillin MICs were 32 and 64 micrograms/ml. Six PBPs were detected in both isolates, demonstrating an apparently increased amount of PBP 5 and decreased penicillin binding of PBPs 1 and 6. These results suggest that ampicillin resistance in the clinical isolates of E. faecalis described could be associated with alterations in different PBPs.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2420-2
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8891156-Ampicillin Resistance,
pubmed-meshheading:8891156-Bacterial Proteins,
pubmed-meshheading:8891156-Carrier Proteins,
pubmed-meshheading:8891156-Enterococcus faecalis,
pubmed-meshheading:8891156-Gram-Positive Bacterial Infections,
pubmed-meshheading:8891156-Hexosyltransferases,
pubmed-meshheading:8891156-Humans,
pubmed-meshheading:8891156-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:8891156-Penicillin-Binding Proteins,
pubmed-meshheading:8891156-Penicillins,
pubmed-meshheading:8891156-Peptidyl Transferases,
pubmed-meshheading:8891156-beta-Lactamases
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pubmed:year |
1996
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pubmed:articleTitle |
Characterization of clinical isolates of beta-lactamase-negative, highly ampicillin-resistant Enterococcus faecalis.
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pubmed:affiliation |
Servicio de Microbiología, Hospital General Universitario Gregorio Marañón, Madrid, Spain.
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pubmed:publicationType |
Journal Article
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