Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-8-30
pubmed:abstractText
Purified membranes of Listeria monocytogenes ATCC 15313 contain at least five penicillin-binding proteins. In two dicloxacillin-resistant mutants, derived from a sensitive parent strain, a 16-fold increase in the MIC of dicloxacillin was observed. A less-significant increase was detected in the MICs of other beta-lactam drugs. In the mutants, PBP 3 lost its strong affinity for dicloxacillin, but remained fully susceptible to binding of 125I-penicillin X, as compared with the wild-type strain. PBP 2 could not be detected in one of the mutants. No decrease in affinity for the radioactive tracer or dicloxacillin was detected in any other PBP of the resistant mutants.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0305-7453
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
751-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Participation of PBP 3 in the acquisition of dicloxacillin resistance in Listeria monocytogenes.
pubmed:affiliation
Departamento de Microbiologia e Inmunologia, Facultad de Farmacia y Bioquimica, Buenos Aires, Argentina.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't