Characterization of an anionic trypsin from the eel (anguilla japonica)

Reiji Yoshinaka, Mamoru Sato, Tohru Suzuki, Shizunori Ikeda

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


1. 1. An enzyme, isolated from the pancreas of the eel Anguilla japonica and designated as anionic trypsin 1, had a molecular weight of 26,000 and an isoelectric point of 5.5. 2. 2. The amino acid composition of the enzyme was similar to that of bovine cationic trypsin as well as anionic trypsins from other species of fish. 3. 3. The enzyme was stable at pH 6 to 9 in the presence of calcium ions. 4. 4. Km and kcat values of the enzyme for N-tosyl-l-arginine methyl ester and N-tosyl-l-lysine methyl ester were quite similar to those of catfish anionic and bovine cationic trypsins.

Original languageEnglish
Pages (from-to)11-14
Number of pages4
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Issue number1
Publication statusPublished - 1985
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology


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