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. 1983 Dec;24(6):925-9.
doi: 10.1128/AAC.24.6.925.

Properties of novel beta-lactamase produced by Bacteroides fragilis

A Yotsuji, S Minami, M Inoue, S Mitsuhashi

Properties of novel beta-lactamase produced by Bacteroides fragilis

A Yotsuji et al. Antimicrob Agents Chemother. 1983 Dec.

Abstract

Bacteroides fragilis strains were isolated from clinical specimens. B. fragilis G-237 was highly resistant to beta-lactam antibiotics due to beta-lactamase production. The purified enzyme from this strain gave a single protein band on polyacrylamide gel electrophoresis. The isoelectric point was 4.8, and the molecular weight was estimated to be 26,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme activity was inhibited by p-chloromercuribenzoate and iodine but not by clavulanic acid or sulbactam. The purified enzyme showed a unique substrate profile by hydrolyzing at a high rate most of the cephalosporins, including cephamycin derivatives, penicillins, and imipenem (formerly imipemide, N-formimidoyl thienamycin, or MK 0787).

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