In vitro activity and beta-lactamase stability of LY163892
- 1 August 1988
- journal article
- research article
- Published by Springer Nature in European Journal of Clinical Microbiology & Infectious Diseases
- Vol. 7 (4) , 549-551
- https://doi.org/10.1007/bf01962613
Abstract
Susceptibility testing of clinical isolates of several gram-negative and gram-positive species showed LY163892 to be more active than cefaclor and cephalexin. OXA-2, TEM-1, TEM-2, PSE-1, CEP-1, CARB-3 and SHV-1 beta-lactamases showed similar activity against LY163892 and cefaclor, whereas OXA-1 hydrolyzed the latter more rapidly. Organisms producing these beta-lactamases, but not TEM-2 and CEP-1, appeared to be more susceptible to LY163892 than cephalexin, although cephalexin proved to be more resistant to beta-lactamase activity. Strains producing TEM-2 and CEP-1 were resistant to LY163892, cefaclor and cephalexin.This publication has 4 references indexed in Scilit:
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