Physiological properties of penicillin-binding proteins in group A streptococci.
We detected five major penicillin-binding proteins (PBPs) in group A streptococci by labeling either cell membrane preparations or live bacteria with tritiated penicillin. All PBPs appeared to be equally accessible to penicillin in vitro and in vivo. Individual PBPs differed in their rates of deacyl...
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| Vydáno v: | Antimicrob Agents Chemother |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1981
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC181537/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7027926/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.19.5.872 |
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