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Structural features related to hydrolytic activity against ceftazidime of plasmid-mediated SHV-type CAZ-5 beta-lactamase.

Tryptic peptides of the novel ceftazidimase CAZ-5 were sequenced by manual Edman degradation and aligned according to strong homology (more than 98%) with SHV-1 and SHV-2 beta-lactamase sequences. CAZ-5 differed from SHV-1 by five amino acid substitutions. Unusually high activity of CAZ-5 towards ce...

Повний опис

Збережено в:
Бібліографічні деталі
Опубліковано в::Antimicrob Agents Chemother
Автори: Péduzzi, J, Barthélémy, M, Tiwari, K, Mattioni, D, Labia, R
Формат: Artigo
Мова:Inglês
Опубліковано: American Society for Microbiology (ASM) 1989
Предмети:
Онлайн доступ:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC172844/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2694955/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.33.12.2160
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