Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. I. Purification, physicochemical properties and structures of fatty acid residues.

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Abstract
An inhibitor of cAMP phosphodiesterase was isolated from the culture filtrate of Bacillus subtilis C-756 isolated from soil. It was purified and finally separated into 3 fractions by reverse-phase HPLC [high-performance liquid chromatography]. The respective fractions were designated as APD[acylpeptide]-I, -II and -III in the order eluted and the relative quantities of APD-I, -II and -III were approximately 10, 40 and 50%, respectively. They were acylpeptides composed of .beta.-hydroxy fatty acid residues and heptapeptide. Though the amino acid compositions of the peptides were the same, the fatty acid residues were different. APD-I contained a mixture of 3-hydroxy-11-methyldodecanoic acid (i-C13H3) and 3-hydroxy-10-methyldodecanoic acid (.alpha.-C13H3). APD-II contained 3-hydroxytetradecanoic acid (.alpha.-C13H3). APD-II contained 3-hydroxytetradecanoic acid (n-C14H3). APD-III contained a mixture of 3-hydroxy-13-methyltetradecanoic acid (i-C15H3) and 3-hydroxy-12-methyltetradecanoic acid (.alpha.-C15H3).