Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I)

• Published in: Biological chemistry Hoppe-Seyler Vol. 371; no. 9; pp. 889 - 895
• Main Authors: Dryjanski, M, Otlewski, J, Polanowski, A, Wilusz, T
• Format: Journal Article
• Language: English
• Published: Germany 01.09.1990
• Subjects: Amino Acid Sequence; Animals; casein; Cattle; Cucurbita ficifolia; enzyme activity; Insulin - metabolism; Kinetics; Molecular Sequence Data; Peptides - metabolism; Plant Proteins - metabolism; purification; seeds; Seeds - enzymology; Serine Endopeptidases - isolation & purification; Serine Endopeptidases - metabolism; serine proteinases; Substrate Specificity; substrates; trypsin inhibitors; Trypsin Inhibitors - metabolism

A proteinase was purified from resting seeds of Cucurbita ficifolia by ammonium sulfate fractionation and successive chromatography on CM-cellulose, (Sephacryl) S-300 and TSK DEAE-2SW (HPLC) columns. Inhibition by DFP and PMSF suggests that the enzyme is a serine proteinase. The apparent molecular m...