Pumpkin (Cucurbita sp.) seed globulin V. Proteolytic activities involved in globulin degradation in ungerminated seeds |
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Authors: | Hara, Ikuko Matsubara, Hiroshi |
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Affiliation: | Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560, Japan |
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Abstract: | Two proteolytic activities I and II involved in the globulindegradation were detected in pumpkin seeds. Activity I, hydrolyzing and ß subunits of the globulin to form Fß,was found in both dry seeds and cycloheximide-treated cotyledons,and decreased during germination. Activity II, hydrolyzing Fßto produce small peptides and amino acids, was not observedin dry seeds but found in cycloheximide-treated cotyledons,increased up to 4 days, and gradually decreased during germination. Activity I gave limited hydrolytic products from the globulinand the chain, but not from Fß, the chain and some animal proteins. It was inhibitedby EDTA. On the other hand, activity II hydrolyzed Fßand the chain faster than the globulin, the chain and some animal proteins. It was inhibitedby EDTA and p-chloromer-curibenzoate, and activated by ß-mercaptoethanol,dithiothreitol and CoCl2. Optimum pH's were at about 6.8 andat 6.0 to 6.8 for activities I and II, respectively. The degradation process of the globulin can be divided intotwo steps: the first step is the conversion of globulin to Fßand the second step, Fß to small peptides and aminoacids. (Received November 9, 1979; ) |
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