Beta-lactamase stability of cefpirome (HR 810), a new cephalosporin with a broad antimicrobial spectrum

@article{Kobayashi1986BetalactamaseSO,
  title={Beta-lactamase stability of cefpirome (HR 810), a new cephalosporin with a broad antimicrobial spectrum},
  author={S. Kobayashi and Susumu Arai and Shoryo Hayashi and K Fujimoto},
  journal={Antimicrobial Agents and Chemotherapy},
  year={1986},
  volume={30},
  pages={713 - 718}
}
Cefpirome was highly stable to hydrolysis by various beta-lactamases, although it was hydrolyzed to some extent by R plasmid-mediated penicillinase of Richmond-Sykes type Va/b and by chromosomal cephalosporinases from Bacteroides species. The compound had a very low affinity for cephalosporinases from Enterobacter cloacae, Citrobacter freundii, Serratia marcescens, and Proteus vulgaris. Cefpirome showed strong antimicrobial activity against eight beta-lactamase (cephalosporinase)-producing… Expand
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