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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| Veröffentlicht in: | Journal of antibiotics 1983, Vol.36(10), pp.1295-1299 |
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| container_end_page | 1299 |
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| container_issue | 10 |
| container_start_page | 1295 |
| container_title | Journal of antibiotics |
| container_volume | 36 |
| creator | KIDO, YASUJI HAMAKADO, TOSHINARI YOSHIDA, TSUTOMU ANNO, MASAMI MOTOKI, YOSHINOBU |
| description | 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. |
| doi_str_mv | 10.7164/antibiotics.36.1295 |
| format | Article |
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Drug treatments ; Physicochemical properties. Structure-activity relationships ; Spectrophotometry ; Streptomyces - growth & development</subject><ispartof>The Journal of Antibiotics, 1983, Vol.36(10), pp.1295-1299</ispartof><rights>Japan Antibiotics Research Association</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c668t-d32e2c4884d349a9b3bfe9d1ed05a5d7a4f74692a0928740144fdfce592251513</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1876,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9673434$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6315666$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KIDO, YASUJI</creatorcontrib><creatorcontrib>HAMAKADO, TOSHINARI</creatorcontrib><creatorcontrib>YOSHIDA, TSUTOMU</creatorcontrib><creatorcontrib>ANNO, MASAMI</creatorcontrib><creatorcontrib>MOTOKI, YOSHINOBU</creatorcontrib><title>ISOLATION AND CHARACTERIZATION OF ANCOVENIN, A NEW INHIBITOR OF ANGIOTENSIN I CONVERTING ENZYME, PRODUCED BY ACTINOMYCETES</title><title>Journal of antibiotics</title><addtitle>J. Antibiot.</addtitle><description>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.</description><subject>actinomycetes</subject><subject>amino acid sequence</subject><subject>Amino Acids - analysis</subject><subject>ancovenin</subject><subject>Angiotensin-Converting Enzyme Inhibitors</subject><subject>Bacteriocins</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Culture Media</subject><subject>General pharmacology</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - pharmacology</subject><subject>Peptides, Cyclic</subject><subject>Pharmacology. 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Antibiot.</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>36</volume><issue>10</issue><spage>1295</spage><epage>1299</epage><pages>1295-1299</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><coden>JANTAJ</coden><abstract>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.</abstract><cop>Tokyo</cop><pub>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</pub><pmid>6315666</pmid><doi>10.7164/antibiotics.36.1295</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-8820 |
| ispartof | The Journal of Antibiotics, 1983, Vol.36(10), pp.1295-1299 |
| issn | 0021-8820 1881-1469 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80766450 |
| source | J-STAGE Free; MEDLINE |
| subjects | 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 |
| title | ISOLATION AND CHARACTERIZATION OF ANCOVENIN, A NEW INHIBITOR OF ANGIOTENSIN I CONVERTING ENZYME, PRODUCED BY ACTINOMYCETES |
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