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Plipastatins have been isolated as part of a program designed to find inhibitors of porcine pancreatic phospholipase A2. They were purified from fermentation broth of Bacillus cereus BMG3O2-fF67 and finally separated into four fractions by reverse phase HPLC. The respective fractions were designated as plipastatins Al, A2, Bl and B2. Plipastatins also inhibited phospholipases C and D. Phospholipase A2 [EC 3.1.1.4] (PL-A2) catalyses the hydrolysis of the fatty acid ester bonds at the 2-position of phospholipids liberating the corresponding free fatty acid and lysophosphatidel). This enzyme has recently received much attention because arachidonic acid released by the reaction is the rate-limiting precursor of inflammatory mediators such as prostaglandins and leukotrienes2). It is also reported to play an important role in the pathogenesis of acute pancreatitis3). As reported in this paper, PL-A2, depending on sources, differ in specificity to inhibitors. Thus, we searched for new PL-A2 inhibitors in culture filtrates of microorganisms. In this communication we report the taxonomy, production, isolation, and characterization of the inhibitors, plipastatins Al, A2, B1 and B2.

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A new antibiotic, setamycin, was extracted from the mycelia of a rare actinomycete strain KM-6054. The antibiotic, the molecular formula of which was found to be C42H91NO12 (tentative), is a yellow powder showing activity against some fungi, trichomonads and weakly against Gram-positive bacteria.