The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
Open accessAbstract
The peptide antibiotic nisin was shown to cause a rapid efflux of amino acids and Rb+ from the cytoplasm of gram-positive bacteria (Staphylococcus cohnii 22, Bacillus subtilis W 23, Micrococcus luteus ATCC 4698, and Streptococcus zymogenes 24). It strongly decreased the membrane potential of cells as judged by the distribution of the lipophilic tetraphenylphosphonium cation. Ascorbate-phenazine methosulfate-driven transport of L-proline by cytoplasmic membrane vesicles was blocked after addition of nisin, and accumulated amino acids were released from the vesicles. Soybean phospholipid (asolectin) vesicles were not affected by nisin. The data suggest that the cytoplasmic membrane is the primary target and that membrane disruption accounts for the bactericidal action of nisin.
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Cites
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Metadata
- Authors
- Ruhr, E., & Sahl, H. G.
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 1985-05
- Volume
- 27
- Issue
- 5
- Pages
- 841-845
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- OpenAlex
- W2172156581
- Cited by
- 375
- References
- 19
- FWCI
- 3.26
- Type
- journal article
- Language
- en
- Open access
- green
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- Ruhr, E., & Sahl, H. G. (1985). Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrobial Agents and Chemotherapy. https://doi.org/10.1128/aac.27.5.841
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
