Ability of cecropin B to penetrate the enterobacterial outer membrane.
The cationic amphipathic insect peptide cecropin B was almost as active on wild-type enteric bacteria as it was on their lipopolysaccharide and lipid A mutants that have very defective outer membrane. The polymyxin-resistant strains, which elaborate altered, less anionic lipopolysaccharide, were com...
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| Gepubliceerd in: | Antimicrob Agents Chemother |
|---|---|
| Hoofdauteurs: | , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1994
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC284773/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7840597/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.38.10.2498 |
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