Isolation and some properties of a serine protease from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam.
An endopeptidase (Cudrania protease) with a molecular mass of 76 kDa has been purified from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam. The enzyme was stable between pH 6 and 10 at 30 degrees C for 60 min. The enzyme activity was inhibited by diisopropyl fluorophosphate, chymostatin, and aprotinin, but not by EDTA or pepstatin. These results indicated that the enzyme was a serine protease.
Uchikoba
T
T
Department of Chemistry, Faculty of Science, Kagoshima University, Japan. uchik@sci.kagoshima-u.ac.jp
Arima
K
K
Shimada
M
M
Yonezawa
H
H
Kaneda
M
M
D005638:Fruit / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010944:Plants / Q000201:enzymology; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
D012697:Serine Endopeptidases