K-582, A NEW PEPTIDE ANTIBIOTIC. I
A new basic peptide antibiotic designated as K-582 was isolated, purified and characterized. When K-582 was applied to a column of Al2O3 or Bio-Gel P-2 or CM Sephadex, two major peaks which were named Fraction I (K-582 A) and Fraction II (K-582 B) were obtained. The nitrogen content, the behavior in...
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| Veröffentlicht in: | Journal of antibiotics 1980, Vol.33(6), pp.533-542 |
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| container_end_page | 542 |
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| container_issue | 6 |
| container_start_page | 533 |
| container_title | Journal of antibiotics |
| container_volume | 33 |
| creator | KONDO, SHIGEJI MEGURIYA, NORIO MOGI, HISAKO AOTA, TOSHINAO MIURA, KENJI FUJII, TOMIO HAYASHI, ICHIRO MAKINO, KORETSUNE YAMAMOTO, MASAHARU NAKAJIMA, NOBUHIRO |
| description | A new basic peptide antibiotic designated as K-582 was isolated, purified and characterized. When K-582 was applied to a column of Al2O3 or Bio-Gel P-2 or CM Sephadex, two major peaks which were named Fraction I (K-582 A) and Fraction II (K-582 B) were obtained. The nitrogen content, the behavior in color reaction, the absorption bands of amide linkages in the infrared absorption spectrum, 1H NMR spectrum and C-13 NMR spectrum indicated the peptide nature of K-582 A and K-582 B. K-582 was effective against yeasts, but inactive against other Gram-positive bacteria, Gram-negative bacteria and Mycobacterium. The toxicity was low in mice. |
| doi_str_mv | 10.7164/antibiotics.33.533 |
| format | Article |
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The nitrogen content, the behavior in color reaction, the absorption bands of amide linkages in the infrared absorption spectrum, 1H NMR spectrum and C-13 NMR spectrum indicated the peptide nature of K-582 A and K-582 B. K-582 was effective against yeasts, but inactive against other Gram-positive bacteria, Gram-negative bacteria and Mycobacterium. 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The toxicity was low in mice.</description><subject>Animals</subject><subject>Anti-Bacterial Agents - isolation & purification</subject><subject>Mice</subject><subject>Microbial Sensitivity Tests</subject><subject>Mitosporic Fungi - metabolism</subject><subject>Neoplasms, Experimental - drug therapy</subject><subject>Peptides - isolation & purification</subject><issn>0021-8820</issn><issn>1881-1469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNj0tLw0AUhQdRaq3-AUEIrk28855Z1hg1tLRdRFwOM8lEU_oiUxf-e1NSSjf3Ls45H3wI3WNIJBbs2W72jWu2-6YMCaUJp_QCDbFSOMZM6Es0BCA4VorANboJYQlAJZVqgAaSYc2EHKLHScwVeYrG0Sz7ihbZoshfs2g8K_KXfF7kaRLlt-iqtqvg745_hD7fsiL9iKfz9zwdT-OSaUJjJ70tLSkFr3AludNgARgB7pgTUkhbE6q9ssQRywUhXLq6AnyolAJA0xEiPbdstyG0vja7tlnb9s9gMAdfc-ZrKDWdbzd66Ee7X7f21WlyFOzySZ8vw95--1Nu246y8udIrIU6YEV_OvqpVf7Y1vgN_QdW2Wl9</recordid><startdate>1980</startdate><enddate>1980</enddate><creator>KONDO, SHIGEJI</creator><creator>MEGURIYA, NORIO</creator><creator>MOGI, HISAKO</creator><creator>AOTA, TOSHINAO</creator><creator>MIURA, KENJI</creator><creator>FUJII, TOMIO</creator><creator>HAYASHI, ICHIRO</creator><creator>MAKINO, KORETSUNE</creator><creator>YAMAMOTO, MASAHARU</creator><creator>NAKAJIMA, NOBUHIRO</creator><general>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>1980</creationdate><title>K-582, A NEW PEPTIDE ANTIBIOTIC. 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I</atitle><jtitle>Journal of antibiotics</jtitle><addtitle>J. Antibiot.</addtitle><date>1980</date><risdate>1980</risdate><volume>33</volume><issue>6</issue><spage>533</spage><epage>542</epage><pages>533-542</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><abstract>A new basic peptide antibiotic designated as K-582 was isolated, purified and characterized. When K-582 was applied to a column of Al2O3 or Bio-Gel P-2 or CM Sephadex, two major peaks which were named Fraction I (K-582 A) and Fraction II (K-582 B) were obtained. The nitrogen content, the behavior in color reaction, the absorption bands of amide linkages in the infrared absorption spectrum, 1H NMR spectrum and C-13 NMR spectrum indicated the peptide nature of K-582 A and K-582 B. K-582 was effective against yeasts, but inactive against other Gram-positive bacteria, Gram-negative bacteria and Mycobacterium. The toxicity was low in mice.</abstract><cop>Japan</cop><pub>JAPAN ANTIBIOTICS RESEARCH ASSOCIATION</pub><pmid>7419467</pmid><doi>10.7164/antibiotics.33.533</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of Antibiotics, 1980, Vol.33(6), pp.533-542 |
| issn | 0021-8820 1881-1469 |
| language | eng |
| recordid | cdi_crossref_primary_10_7164_antibiotics_33_533 |
| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese |
| subjects | Animals Anti-Bacterial Agents - isolation & purification Mice Microbial Sensitivity Tests Mitosporic Fungi - metabolism Neoplasms, Experimental - drug therapy Peptides - isolation & purification |
| title | K-582, A NEW PEPTIDE ANTIBIOTIC. I |
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