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Journal of Antimicrobial Chemotherapy (1985) 16, 297-304
© 1985 The British Society for Antimicrobial Chemotherapy

research-article

Purification and properties of a ß-lactamase from Alcaligenes dentrificans subsp. xylosoxydans

Tadashi Fujii*, Kenichi Sato*, Matsuhisa Inoue{dagger} and Susumu Mitsuhashi*

*Episome Institute, Fujimi-mura Seta-gun, Gunma, Japan {dagger}Laboratory of Drug Resistance in Bacteria, School of Medicine Gunma University, Maebashi, Japan

accepted 17 April 1985

A penicillin ß-lactamase was purified from a strain of Alcaligenes dentrificans subsp. xylosoxydans resistant to ß-lactam antibiotics. The purified enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis, and its molecular weight was 18,000 from sodium dodecylsulphate-acrylamide gel electrophoresis and gel filtration. Its isoelectric point was 9·8, the optimal pH was 8·5 and the optimal temperature was 35°C.

The enzyme hydrolyzed penicillin G and ampicillin more rapidly than cephalo-sporins. Relative rates, with penicillin G as 100, were: ampicillin, 102; carbenicillin, 15; cloxacillin, >1; piperacillin, 9; cephaloridine, 41; cefoperazone, 36; cefpiramide, 36 and cefmenoxime, 14.

Clavulanic acid, sulbactam, imipenem, and cephamycins had low affinities for the enzyme.

The enzyme activity was inhibited by iodine, Hg2+, clavulanic acid and sulbactam.


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