ISOLATION AND CHARACTERIZATION OF ANCOVENIN, A NEW INHIBITOR OF ANGIOTENSIN I CONVERTING ENZYME, PRODUCED BY ACTINOMYCETES

Ancovenin, an inhibitor of angiotensin I converting enzyme isolated from the culture broth of a Streptomyces species, is a dialysable peptide composed of sixteen amino acid residues containing unusual amino acids such as threo-β-methyllanthionine, meso-lanthionine, and dehydroalanine.

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Bibliographische Detailangaben
Veröffentlicht in:	Journal of antibiotics 1983, Vol.36(10), pp.1295-1299
Hauptverfasser:	KIDO, YASUJI, HAMAKADO, TOSHINARI, YOSHIDA, TSUTOMU, ANNO, MASAMI, MOTOKI, YOSHINOBU
Format:	Artikel
Sprache:	eng
Schlagworte:	actinomycetes amino acid sequence Amino Acids - analysis ancovenin Angiotensin-Converting Enzyme Inhibitors Bacteriocins Biological and medical sciences Chromatography, High Pressure Liquid Culture Media General pharmacology Kinetics Medical sciences Microbial Sensitivity Tests Peptides - isolation & purification Peptides - pharmacology Peptides, Cyclic Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Spectrophotometry Streptomyces - growth & development
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Beschreibung
Zusammenfassung:	Ancovenin, an inhibitor of angiotensin I converting enzyme isolated from the culture broth of a Streptomyces species, is a dialysable peptide composed of sixteen amino acid residues containing unusual amino acids such as threo-β-methyllanthionine, meso-lanthionine, and dehydroalanine.
ISSN:	0021-8820 1881-1469
DOI:	10.7164/antibiotics.36.1295