Abstract
The stability to beta-lactamase hydrolysis of HR 756, a new cephalosporin antibiotic, was compared to the beta-lactamase stability of cefoxitin and cefuroxime. HR 756, cefoxitin, and cefuroxime were not hydrolyzed by Richmond type I, III, IV, and V beta-lactamases. Antibacterial activity of HR 756 correlated well with resistance to beta-lactamase hydrolysis except against Pseudomonas aeruginosa. HR 756, cefoxitin, and cefuroxime inhibited type I beta-lactamases, but not type III, IV, or V enzymes. HR 756 was the most active inhibitor.
MeSH Terms
Cephalosporins/pharmacology
Drug Resistance, Microbial
Pseudomonas aeruginosa/drug effects
beta-Lactamase Inhibitors
Chemicals
Cephalosporins
beta-Lactamase Inhibitors
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fu K P
Neu H C
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13 references, click to expand
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