Abstract
Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29,000). Their specificity spectrum was rather wide, since they hydrolysed some cephalosporins with kcat: values similar to those observed with the best penicillin substrates. Cloxacillin, methicillin and imipenem were hydrolysed very slowly. Hydrolysis of azthreonam could not be detected.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / analysis
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Cephalosporins / metabolism
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Chromatography, Affinity
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Chromosomes, Bacterial / enzymology
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Citrobacter / enzymology*
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Electrophoresis, Polyacrylamide Gel
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Isoelectric Point
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Isoenzymes / isolation & purification*
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Kinetics
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Molecular Weight
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Penicillins / metabolism
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Substrate Specificity
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beta-Lactamases / isolation & purification*
Substances
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Amino Acids
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Cephalosporins
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Isoenzymes
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Penicillins
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beta-Lactamases