| Literature DB >> 6975269 |
R J Mehta, D J Newman, B A Bowie, C H Nash, P Actor.
Abstract
The stability of cefonicid (SK&F 75073) towards representatives of six major classes of beta-lactamases was determined using a spectrophotometric assay. Cefonicid was stable to hydrolysis by the Type I enzyme from Enterobacter cloacae and by the enzyme from the anaerobe, Bacteroides fragilis. It was 6 to 7 times more stable than cefamandole to the Type IIIA and B enzymes from Escherichia coli, a little less stable than this antibiotic to the Type V enzyme from E. coli, and of equal stability to the Type IV enzyme from Klebsiella aerogenes. Cefonicid was a non-competitive inhibitor (Ki of 0.8 x 10(-6)M) of cephalothin hydrolysis by the Type I enzyme.Entities:
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Year: 1981 PMID: 6975269 DOI: 10.7164/antibiotics.34.202
Source DB: PubMed Journal: J Antibiot (Tokyo) ISSN: 0021-8820 Impact factor: 2.649