Inhibition and Accelerated Autolysis of Trypsin due to Incorporation of Polymer of Oxidized Methyl Linolenate

Abstract

Bovine trypsin (EC 3.4.4.4) allowed to react with [¹⁴C] polymer of oxidized methyl linolenate (oxd MLn) was analyzed by chromatography on Sephadex G-75, Sephadex G-25 and SP-Sephadex C-25. The incorporation of [¹⁴C] polymer was observed in high molecular weight fraction corresponding to trypsin molecule and low molecular weight fraction, decomposed products of trypsin. On the other hand, acetyltrypsin prepared by the modification of ε-amino groups in trypsin did not incorporate the polymer, so it was found that the incorporation was based on the carbonylamine condensation reaction. The polymer inhibited α- and β-trypsin definitely among trypsin derivatives and by reaction produced the inactive complexes. The complexes were easily decomposed by active trypsin and converted to low molecular weight fragments. So the authors concluded that the occurrence of the inhibitory effect of the polymer depended on the production of the inactive complexes but not on the acceleration of autolysis, which was the secondary phenomenon of the decomposed complexes.