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Purification and characterization of aseanostatins: actinomycete-derived fatty acid inhibitors to myeloperoxidase release from human polymorphonuclear leukocytes.
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- ISHIDA-OKAWARA AKIKO
- Department of Antibiotics, National Institute of Health
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- KIMOTO YUKIO
- Department of Antibiotics, National Institute of Health
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- WATANABE KAZUO
- Sagami Chemical Research Center
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- TOKUDA KOICHI
- Department of Antibiotics, National Institute of Health
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- SHIBATA MICHIO
- Department of Antibiotics, National Institute of Health Department of Biology, Faculty of Science, Tokyo Metropolitan University
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- MASUDA KAORI
- Department of Antibiotics, National Institute of Health
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- TAKANO YUKIE
- Department of Antibiotics, National Institute of Health
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- KAWAGUCHI KAZUE
- Department of Antibiotics, National Institute of Health
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- AKAGAWA HISAYOSHI
- Department of Antibiotics, National Institute of Health
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- NILUBOL NALINE
- The Institute of Biotechnology and Genetic Engineering, Chulalongkorn University
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- HOTTA KUNIMOTO
- Department of Antibiotics, National Institute of Health
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- YAZAWA KAZUNAGA
- Sagami Chemical Research Center
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- MIZUNO SATOSHI
- Department of Antibiotics, National Institute of Health
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- SUZUKI KAZUO
- Department of Antibiotics, National Institute of Health
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Description
We found inhibitors, designated aseanostatins PI and P5, against myeloperoxidase (MPO) release from human polymorphonuclear leukocytes (PMN). Aseanostatins were extracted from an actinomycete isolated in Thailand and purified by a series of column chromatography of charcoal and silica gel, and HPLC. Physico-chemical characterization by gas liquid chromatography and GC-MS indicated that aseanostatins were fatty acids. The active forms of aseanostatins were recovered by hydrolyzing their methyl esters after HPLC. Two components PI and P5 with the IC50 of 0.96 and 0.54μg/ml to the MPO release were obtained as pure forms, indicating aseanostatin P5 was higher activity than aseanostatin PI. The component PI was identical with 12-methyltridecanoic acid and P5 was indistinguishable to 12-methyltetradecanoic acid (ante-i-15:0). Aseanostatin P5 (1μg/ml) did not inhibit β-glucuronidase release, but O2- production a little. It has no effect on chemotaxis of PMN to fMet-Leu-Phe (10-8M), PMN adhesion or phosphorylation of a 64-kD protein in the PMN cell-lysate system.
Journal
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- The Journal of Antibiotics
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The Journal of Antibiotics 44 (5), 524-532, 1991
JAPAN ANTIBIOTICS RESEARCH ASSOCIATION
