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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-7-5
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pubmed:abstractText |
Aminoglycoside resistance was investigated in six clinical isolates of Stenotrophomonas (Xanthomonas) maltophilia by studying the uptake kinetics and by using a radiochemical method to detect aminoglycoside modifying enzymes. Furthermore, the lipopolysaccharides (LPS) were extracted and characterized by SDS-PAGE and chemical analysis. Dansyl-polymyxin displacement experiments confirmed the availability of anionic binding sites. Growing cells of the isolates bound dansyl-polymyxin but were not lysed.
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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 |
Jan
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pubmed:issn |
0305-7453
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
167-71
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:7768765-Aminoglycosides,
pubmed-meshheading:7768765-Anti-Bacterial Agents,
pubmed-meshheading:7768765-Bacterial Outer Membrane Proteins,
pubmed-meshheading:7768765-Binding Sites,
pubmed-meshheading:7768765-Drug Resistance, Microbial,
pubmed-meshheading:7768765-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7768765-Lipopolysaccharides,
pubmed-meshheading:7768765-Polymyxins,
pubmed-meshheading:7768765-Xanthomonas
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pubmed:year |
1995
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pubmed:articleTitle |
The role of lipopolysaccharide anionic binding sites in aminoglycoside uptake in Stenotrophomonas (Xanthomonas) maltophilia.
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pubmed:affiliation |
Pasteur Institute of Brabant, Antibiotic Research Unit, Brussels, Belgium.
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pubmed:publicationType |
Journal Article
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