title: Isolation and some properties of a serine protease from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam.
abstract: 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.
authors.affiliation: Department of Chemistry, Faculty of Science, Kagoshima University, Japan. uchik@sci.kagoshima-u.ac.jp
authors.forename: T
authors.initials: T
authors.lastname: Uchikoba
authors.forename: K
authors.initials: K
authors.lastname: Arima
authors.forename: M
authors.initials: M
authors.lastname: Shimada
authors.forename: H
authors.initials: H
authors.lastname: Yonezawa
authors.forename: M
authors.initials: M
authors.lastname: Kaneda
mesh_terms: D005638:Fruit / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010944:Plants / Q000201:enzymology; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013696:Temperature
chemical_list: D012697:Serine Endopeptidases