The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
PROPERTIES OF A BROAD SPECTRUM β-LACTAMASE ISOLATED FROM FLAVOBACTERIUM MENINGOSEPTICUM GN14059
TADASHI FUJIIKENICHI SATOEISAKU YOKOTATETSURO MAEJIMAMATSUHISA INOUESUSUMU MITSUHASHI
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1988 Volume 41 Issue 1 Pages 81-85

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Abstract

A broad substrate-spectrum β-lactamase was purified from Flavobacterium meningosepticum GN14059. The purified enzyme gave a single protein band on SDS-polyacrylamide gel electrophoresis. The molecular weight was estimated to be about 30, 000 and the isoelectric point was 5.1.
The enzyme hydrolyzed various β-lactam antibiotics including oxyiminocephalosporins and aztreonam. Relative rates, with cephaloridine as 100, were cephalothin 200, cefazolin 48, cefuroxime 153, cefotaxime 51, ceftazidime 20, ampicillin 26, carbenicillin 19, and aztreonam 20.
The enzyme activity was inhibited by clavulanic acid, sulbactam, imipenem and cephamycins.

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