Purification and some properties of two anionic trypsins from the eel (anguilla japonica)

Reiji Yoshinaka, Mamoru Sato, Tohru Suzuki, Shizunori Ikeda

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


1. 1. Two anionic enzymes, designated as trypsins 1 and 2, were purified from the pancreas of the eel Anguilla japonica by DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. 2. 2. The final preparation of trypsin 1 was homogeneous but that of trypsin 2 still contained impurities. 3. 3. Both enzymes had similar pH optima of near 8.3 for the hydrolysis of N-tosyl-l-arginine methyl ester. 4. 4. Trypsin 1 was stabilized by calcium ions but the stability of trypsin 2 was not affected by calcium ions. 5. 5. Both enzymes were inhibited by typical trypsin inhibitors including serine proteinase inhibitors.

Original languageEnglish
Pages (from-to)5-9
Number of pages5
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Issue number1
Publication statusPublished - 1985
Externally publishedYes


  • 02041984

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology


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