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Identification of CMY-2-type cephalosporinases in clinical isolates of Enterobacteriaceae by MALDI-TOF MS
CC. Papagiannitsis, SD. Kotsakis, Z. Tuma, M. Gniadkowski, V. Miriagou, J. Hrabak,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1972 do Před 6 měsíci
Freely Accessible Science Journals
od 1995 do Před 6 měsíci
PubMed Central
od 1972 do Před 6 měsíci
Europe PubMed Central
od 1972 do Před 6 měsíci
Open Access Digital Library
od 1972-01-01
Open Access Digital Library
od 1972-01-01
PubMed
24566177
DOI
10.1128/aac.02418-13
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny metabolismus MeSH
- cefalosporinasa metabolismus MeSH
- Enterobacteriaceae enzymologie MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice metody MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
This study exploited the possibility to detect Citrobacter freundii-derived CMY-2-like cephalosporinases in Enterobacteriaceae clinical isolates using matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). Periplasmic proteins were prepared using a modified sucrose method and analyzed by MALDI-TOF MS. A ca. 39,850-m/z peak, confirmed to represent a C. freundii-like β-lactamase by in-gel tryptic digestion followed by MALDI-TOF/TOF MS, was observed only in CMY-producing isolates. We have also shown the potential of the assay to detect ACC- and DHA-like AmpC-type β-lactamases.
Citace poskytuje Crossref.org
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