Beta-Lactamase Stability of HR 756, a Novel Cephalosporin, Compared to That of Cefuroxime and Cefoxitin
Kwung P. Fu, Harold C. Neu
Abstract
Kwung P. Fu, Harold C. Neu
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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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.
Key concepts: Cefoxitin, Cefuroxime, Cephalosporin, Microbiology, Beta-lactamase, Pseudomonas aeruginosa, Antibiotics, Chemistry