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Antimicrobial Agents and Chemotherapy, Jul 1995, 1458-1461, Vol 39, No. 7
Copyright © 1995 by the American Society for Microbiology. All rights reserved.

Purification and characterization of a new beta-lactamase from Bacteroides uniformis

M Hedberg, L Lindqvist, T Bergman and CE Nord
Department of Immunology, Microbiology, Pathology, and Infectious Diseases, Huddinge University Hospital, Sweden.

A beta-lactam-resistant Bacteroides uniformis strain was isolated from a clinical specimen. The strain produced large amounts of beta- lactamase and was resistant to penicillins and cephalosporins. The specific activity of the unpurified beta-lactamase was 4.8 U/mg of protein with nitrocefin as the substrate. The enzyme was purified 188- fold by Q-Sepharose, Sephacryl S-300, and Mono Q column passages. Kinetic parameters of the enzyme were determined by a micromethod performed in microtiter plates. beta-Lactamase was inhibited by cefoxitin and imipenem and hydrolyzed cephalosporins more rapidly than penicillins. The molecular weight was determined by sodium dodecyl sulfate-gradient gel electrophoresis to be 32,500, and the isoelectric point was 4.5.


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