Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I)
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...
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Published in | Biological chemistry Hoppe-Seyler Vol. 371; no. 9; pp. 889 - 895 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Germany
01.09.1990
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Subjects | |
Online Access | Get more information |
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