自動酸化リノレン酸メチルの分解生成物によるトリプシンのアミダーゼ活性促進

抄録

Methyl linolenate autoxidized at 40°C for 4 days in the dark was separated into polymers, monomers and degradation products by chromatography on a Sephadex LH-20 column. Each fraction eluted was allowed to react with bovine pancreatic β-trypsin at 37°C, pH 8.0 for 1h. The change in amidase activity of the reaction mixture was then observed using α-N-benzoyl-_DL-arginine-p-nitroanilide as a substrate. Among the fractions obtained, amidase activity was obviously accelerated by a group of degradation products (DP II). The interaction between DP II and trypsin was thus further studied and the following information obtained : (1) the action of DP II to accelerate amidase activity was caused by reaction of DP II with trypsin but not with the substrate; (2) neither the esterase nor proteinase activity of trypsin was accelerated by the reaction of DP II with trypsin nor was there any change in substrate specificity; (3) the reaction between the carbonylgroups of DP II and ε-amino groups of trypsin was essential for the occurrence of the accelerating action of DP II on the amidase activity of trypsin.