Abstract
The hydrolysate of iturin C contains α-aminoacids and liposoluble β-aminoacids in the same molar ratios as in iturin A. Electrophoretic migration and alkaline titration indicate the presence of one carboxyl group in iturin C. The reduction of iturin C with diborane shows that this carboxyl group in in an aspartyl residue. The sequence was determined by mass spectrometry of permethylated iturin C in comparison with mass spectrometry of permethylated iturin A. The aspartyl residue is linked to the carboxyl group of the β-aminoacid. In addition, a liposoluble compound seryl→β-aminoacid was isolated from partial hydrolysis which confirmed the cyclic structure of iturin C. In contrast to iturin A, iturin C has no antibiotic activity.
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