Enzymatic characterization of anionic trypsin of the catfish (Parasilurus asotus)

Reiji Yoshinaka, Mamoru Sato, Tohru Suzuki, Shizunori Ikeda

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

Abstract

1. 1. An anionic trypsin, isolated from the pancreatic extract of the catfish (Parasilurus asotus), had a pH optimum of 8.3 for the hydrolysis of N-tosyl-l-arginine methyl ester. 2. 2. The enzyme was most stable at pH 6.0-8.5, and was stabilized by calcium ions. 3. 3. The enzyme was inhibited by typical trypsin inhibitors including some serine proteinase inhibitors. 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 bovine cationic trypsin.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume77
Issue number1
DOIs
Publication statusPublished - 1984
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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