Purification and properties of a cephalosporinase from Enterobacter cloacae.

Antimicrobial Agents and Chemotherapy
S MinamiS Mitsuhashi

Abstract

A cephalosporin beta-lactamase (cephalosporinase) was extracted from Enterobacter cloacae GN7471 and purified by means of column chromatography. The resulting preparation gave a single protein band upon polyacrylamide gel electrophoresis. The enzyme's isoelectric point was 8.4, and its molecular weight was 44,000. The optimal pH was 8.5, and the optimal temperature was 40 degrees C. The enzyme hydrolyzed cephalosporins much more readily than penicillins. The enzyme activity was inhibited by iodine, semisynthetic penicillins, cefuroxime-type cephalosporins, and cephamycin derivatives. The enzymological properties of the purified enzyme were compared with those of beta-lactamases derived from other gram-negative enteric bacteria.

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Citations

Mar 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·R F Pratt, C P Govardhan
Aug 1, 1982·Antimicrobial Agents and Chemotherapy·K KatsuS Mitsuhashi
Apr 1, 1985·Antimicrobial Agents and Chemotherapy·M TodaA Tachibana
Nov 1, 1986·Antimicrobial Agents and Chemotherapy·S KobayashiK Fujimoto
Jul 1, 1987·Antimicrobial Agents and Chemotherapy·Y UtsuiS Mitsuhashi
Sep 1, 1988·Antimicrobial Agents and Chemotherapy·A TamuraS Mitsuhashi
Mar 1, 1989·Antimicrobial Agents and Chemotherapy·K Bush
Apr 1, 1990·Antimicrobial Agents and Chemotherapy·H MatsuiS Mitsuhashi
Dec 1, 1995·Antimicrobial Agents and Chemotherapy·Y WatanabeH Ochiai
Feb 19, 2000·Antimicrobial Agents and Chemotherapy·A KugaM Inoue
Jan 13, 2009·Clinical Microbiology Reviews·George A Jacoby
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Dec 1, 1984·Acta Pathologica, Microbiologica, Et Immunologica Scandinavica. Section B, Microbiology·P Søgaard
Jul 1, 1986·Drug Intelligence & Clinical Pharmacy·D L Dworzack

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