Author:
Sahl H G,Grossgarten M,Widger W R,Cramer W A,Brandis H
Abstract
The staphylococcin-like peptide Pep-5 was shown to be a complex mixture of closely related and strongly basic peptides. Five peptides were purified by high-pressure liquid chromatography on reversed-phase and gel filtration columns and further characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino acid analysis. Four peptides have molecular weights of ca. 3,500, whereas one is of double size. All contain the thioether amino acid lanthionine and a large number of lysine residues per molecule. The amino terminus of the main active peptide is blocked; the carboxy-terminal end is formed by a lysine residue. The data obtained for Pep-5 suggest striking structural similarities to the peptide antibiotics nisin and subtilin.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Reference15 articles.
1. Allen G. 1981. Sequencing of proteins and peptides. Elsevier/North Holland Biomedical Press Amsterdam.
2. The number and nature of a, p-unsaturated amino acids in subtilin;Gross E.;Biochem. Biophys. Res. Commun.,1973
3. Subtilin;Gross E.;IV. Die Struktur des Subtilins. Hoppe-Seyler's Z. Physiol. Chem.,1973
4. The presence of dehydroalanine in the antibiotic nisin and its relationship to activity;Gross E.;J. Am. Chem. Soc.,1967
5. Nisin. The assignment of sulfide bridges of P-methyl-lanthionine to a novel bicyclic structure of identical ring size;Gross E.;J. Am. Chem. Soc.,1970
Cited by
59 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献