Three beta-lactamases isolated from Aeromonas salmonicida, including a carbapenemase not detectable by conventional methods.

Abstract	The beta-lactamases of seven strains of Aeromonas salmonicida subsp. achromogenes resistant to amoxicillin (MIC > 1024 mg/l) and responsible for furunculosis in farmed Atlantic salmon in Scotland were examined to establish the mechanisms of beta-lactam resistance. Separation of a cell-free extract on an isoelectric focusing gel stained with the chromogenic cephalosporin nitrocefin showed the presence of two beta-lactamases, one with a pI of 7.9 and the other with a pI of 6.0. Hydrolysis assays of cell-free extracts of these strains demonstrated carbapenemase, penicillinase and cephalosporinase activity. However, when the beta-lactamases were separated by anion exchange chromatography, the carbapenemase activity could not be retrieved in either of the peak fractions containing the separated enzymes that had been visualised by nitrocefin. Consequently, a novel carbapenemase was discovered which cannot be detected with nitrocefin.
Authors	M V Hayes, C J Thomson, S G Amyes
Journal	European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology (Eur J Clin Microbiol Infect Dis) Vol. 13 Issue 10 Pg. 805-11 (Oct 1994) ISSN: 0934-9723 [Print] Germany
PMID	7889949 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Anti-Bacterial Agents Bacterial Proteins Amoxicillin beta-Lactamases carbapenemase
Topics	Aeromonas (drug effects, enzymology, isolation & purification) Amoxicillin (pharmacology) Animals Anti-Bacterial Agents (pharmacology) Bacterial Proteins Bacteriological Techniques Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Fish Diseases (microbiology) Furunculosis (microbiology, veterinary) Isoelectric Focusing Microbial Sensitivity Tests Molecular Weight Salmon (microbiology) Substrate Specificity beta-Lactam Resistance beta-Lactamases (isolation & purification, metabolism)

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