Affiliation:
1. Institut für Medizinische Mikrobiologie und Immunologie der Universität Bonn, Federal Republic of Germany.
Abstract
Staphylococcin 1580 was purified to homogeneity from culture supernatants of Staphylococcus epidermidis 1580 by means of adsorption to XAD 2, cation exchange chromatography, and high-performance liquid chromatography on reversed-phase C18. The purified active substance migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent M(r) of approximately 2,000. Amino acid analysis, mass determination (2,165 Da) and N-terminal sequencing (Ile-Ala-Xaa-Lys-Phe-Ile-Xaa-Xaa-Pro-Gly-Xaa-Ala-Lys-block) demonstrated that staphylococcin 1580 is identical to epidermin, a lanthionine-containing antibiotic peptide (lantibiotic).
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Reference37 articles.
1. Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic;Allgaier H.;Eur. J. Biochem.,1986
2. Bayer A. S. Freund C. Nicholson and G. Jung. Postranslational backbone modifications in the ribosomal biosynthesis of the glycine-rich antibiotic microcin B17. Angew. Chem. Int. Ed. Engl. in press.
3. Benz R. G. Jung and H. G. Sahl. 1991. Mechanism of channelformation by lantibiotics in black lipid membranes p. 359-372. In G. Jung and H. G. Sahl (ed.) Nisin and novel lantibiotics. Escom Leiden The Netherlands.
4. Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes;Bierbaum G.;Arch. Microbiol.,1985
5. Bactericidal substance from Staphylococcus aureus;Dajani A. S.;J. Exp. Med.,1970
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37 articles.
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