Abstract
A substance which accelerates the amidase activity of trypsin by more than three times that of intact trypsin was separated from autoxidized methyl linolenate by gel chromatography on Sephadex LH- 20, silicic acid chromatography on Silica gel 60, and by high-performance liquid chromatography on μ-Porasil. This substance isolated from the highly active fraction was identified as methyl 12-oxo-9-hydroxy-10-dodecenoate by GLC and GC-MS analyses.
