Premium
Isolation of two chymotrypsins from grass carp
Author(s) -
Fong WingPing,
Chan Elaine YeeMan,
Lau KingKwan
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202792
Subject(s) - chymotrypsin , chemistry , sepharose , trypsin , phenylalanine , aprotinin , protease , chromatography , amide , biochemistry , enzyme , amino acid , medicine
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.