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Isolation and some properties of a serine protease from the fruits of Cudrania cochinchinensis (Lour.) Kudo et Masam
Authors:Uchikoba T  Arima K  Shimada M  Yonezawa H  Kaneda M
Institution:Department of Chemistry, Faculty of Science, Kagoshima University, Japan. uchik@sci.kagoshima-u.ac.jp
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.
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