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.
|Number of pages||6|
|Journal||Comparative Biochemistry and Physiology -- Part B: Biochemistry and|
|Publication status||Published - 1984|
ASJC Scopus subject areas
- Molecular Biology