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Extracts prepared from endosperms of germinating seeds of Scots pine, Pinus sylvestris L., rapidly hydrolysed the β‐naphthylamides of L‐phenylalanine and L‐leucine optimally at pH 6.5 and that of L‐arginine at pH 7.7. Disc electrophoresis followed by activity staining showed that the activities were due to two naphthylamidases (aminopeptidases) with different substrate specificities. Seeds were allowed to germinate at 20°C on agar gel in the dark and the activities on the three substrates were assayed from separated endosperms and seedlings at various stages of germination. The activities in the endosperm of resting seeds were relatively high and they remained unchanged throughout the period of reserve protein mobilization (seedling length up to 50 mm), after which they began to decrease. The activities of the naphthylamidases are rather small compared with those of the two alkaline peptidases of pine, contributing about 17% of the total amino‐peptidase activity in the endosperm of germinating seeds. The total aminopeptidase activity is sufficient to account for the rate of storage protein mobilization during germination. In the seedlings the naphthylamidase activities (per seedling) increased continuously during germination, and activities per g dry weight were higher than those in the endosperm.
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Salmia et al. (1976) studied this question.
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