Isolation and partial characterization of a protease from Cucurbita ficifolia
- 30 January 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 243 (2) , 363-365
- https://doi.org/10.1016/0014-5793(89)80162-0
Abstract
A protease from the pulp of Cucurbita ficifolia was purified. Its molecular mass was estimated to be about 60 kDa. Its maximum activity is in the alkaline region against azocollagen as substrate. The enzyme is inhibited by phenylmethylsulphonyl fluoride but not by EDTA and iodoacetic acid.Keywords
This publication has 7 references indexed in Scilit:
- Photochemical oxidation of cucumisin, a serine proteinase from Cucumis melo.Agricultural and Biological Chemistry, 1987
- Isolation and characterization of a proteinase from white gourdPhytochemistry, 1977
- Isolation and Characterization of a Proteinase from the Sarcocarp of Melon FruitThe Journal of Biochemistry, 1975
- Use of azo-dye-bound collagen to measure reaction velocities of proteolytic enzymesAnalytical Biochemistry, 1969
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- Sulfonyl Fluorides as Inhibitors of Esterases. III. Identification of Serine as the Site of Sulfonylation in Phenylmethanesulfonyl α-Chymotrypsin*Biochemistry, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951