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. 1978 Sep;14(3):322-6.
doi: 10.1128/AAC.14.3.322.

beta-lactamase stability of HR 756, a novel cephalosporin, compared to that of cefuroxime and cefoxitin

K P Fu, H C Neu

beta-lactamase stability of HR 756, a novel cephalosporin, compared to that of cefuroxime and cefoxitin

K P Fu et al. Antimicrob Agents Chemother. 1978 Sep.

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.

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