Characterization of binding sites for a bacteriocin produced by Mycobacterium smegmatis.
A bacteriocin from Mycobacterium smegmatis ATCC 14468 which adsorbed to the cell wall-enriched fraction and the crude lipopolysaccharide preparation from Mycobacterium diernhoferi ATCC 19340 was inhibited by D-glucose and alpha-linked glucosylated derivatives.
Uloženo v:
| Vydáno v: | J Bacteriol |
|---|---|
| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1980
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC294676/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7419493/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.144.1.428-431.1980 |
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