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

Authors
  • Hedberg, M
  • Lindqvist, L
  • Bergman, T
  • Nord, C E
Type
Published Article
Journal
Antimicrobial agents and chemotherapy
Publication Date
Jul 01, 1995
Volume
39
Issue
7
Pages
1458–1461
Identifiers
PMID: 7492085
Source
Medline
License
Unknown

Abstract

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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