doi: 10.1128/AAC.35.2.371.
Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis
Affiliations
- PMID: 1902649
- PMCID: PMC245008
- DOI: 10.1128/AAC.35.2.371
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Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis
Antimicrob Agents Chemother.
1991 Feb.
Abstract
The beta-lactamase from Bacteroides fragilis GAI-30144 hydrolyzed imipenem, oxyiminocephalosporins, cephamycins, and penicillins. Enzyme activity was inhibited by EDTA. Zinc completely reversed inactivation of the enzyme by EDTA. The molecular mass of purified enzyme was estimated to be 33,000 daltons.
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