Affordable Access

Isolation of two chymotrypsins from grass carp.

Authors
  • Fong, W P
  • Chan, E Y
  • Lau, K K
Type
Published Article
Journal
Biochemistry and molecular biology international
Publication Date
Jun 01, 1998
Volume
45
Issue
2
Pages
409–418
Identifiers
PMID: 9678263
Source
Medline
License
Unknown

Abstract

Two chymotrypsins were purified from the hepatopancreas of grass carp (Ctenopharyngodon idellus) by chromatographies on phenyl-Sepharose and Q-Sepharose. The molecular weights of chymotrypsins I and II were 28 and 27 kDa, respectively. The two chymotrypsins showed similar susceptibility to inhibitions by phenylmethylsulfonyl fluoride and soybean trypsin inhibitor, but differed in their response to tosyl-L-phenylalanine chloromethyl ketone and aprotinin in which chymotrypsin I was more resistant. Chymotrypsin I was a less typical chymotrypsin and exhibited lower catalytic efficiency with the chymotrypsin-specific ester and amide substrates, when compared with chymotrypsin II. For both chymotrypsins, optimal activity was detected in the pH range 7.0-8.5.

Report this publication

Statistics

Seen <100 times