Acceleration of Autolysis of Trypsin by Oxidized Methyl Linolenate

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  • Hatate Hideo
    Laboratory or Fisheries Technology, Faculty of Agriculture, Kyushu University
  • Toyomizu Masamichi
    Laboratory or Fisheries Technology, Faculty of Agriculture, Kyushu University

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  • 酸化リノレン酸メチルによるtrypsinの自己分解促進
  • サンカ リノレンサン メチル ニ ヨル trypsin ノ ジコ ブンカイ ソ

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Abstract

methyl linolenate (oxd MLn) or the polymer fractionated from oxd MLn. The results obtained are summarized as follows. 1. The decrease in trypsin was observed in Sephadex G-100 chromatogram after the reaction with oxd MLn, but polymerized trypsin was not detected. 2. The remarkable decrease in α-and β-trypsin, main active derivatives of trypsin, and the increase in the other derivatives, designated as unidentified trypsin and trypsin Ⅰ in the text, were observed in SP-Sephadex C-25 chromatogram after the reaction with oxd MLn. The latter derivatives were contaminated with the low molecular weight fractions derived from trypsin. On the other hand, by the reaction with the polymer, α-andβ-trypsin also decreased as observed in the case of oxd MLn, but the increase in unidentified trypsin and trypsin I was not so large as by the reaction with oxd MLn. 3. By the reaction with the polymer, trypsin increased in C-terminal amino acid residues (Lys and/or Arg) owing to the autolysis of trypsin. The increase of C-terminal amino acid residues was parallel to the inhibition of trypsin. From these results, the authors supposed that the autolysis of trypsin was accelerated by the reaction with oxd MLn or the polymer.

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