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High level expression of a frog α-amidating enzyme, AE-II, in cultured cells and silkworm larvae using aBombyx mori nuclear polyhedrosis virus expression vector

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Abstract

AXenopus laevis peptidyl C-terminal α-amidating enzyme (AE-II) gene, modified by deletion of a region encoding the putative membrane-spanning domain and the putative C-terminal cytosolic tail, was expressed in BoMo-15 AIIc insect cells and silkworm larvae using aBombyx mori baculovirus expression vector system. The expressed enzyme was identified predominantly in the culture medium and the hemolymph of silkworm larvae, indicating successful secretion of the expressed AE-II. The level of recombinant enzyme in the larval hemolymph at 4 days post-infection (40 μg/ml) was more than 100-fold the peak levels found in the culture medium (250 ng/ml). The enzyme activity in the larval hemolymph at 4 days post-infection was 3700 units/ml.

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Kobayashi, J., Imanishi, S., Inoue, H. et al. High level expression of a frog α-amidating enzyme, AE-II, in cultured cells and silkworm larvae using aBombyx mori nuclear polyhedrosis virus expression vector. Cytotechnology 8, 103–108 (1992). https://doi.org/10.1007/BF02525492

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  • DOI: https://doi.org/10.1007/BF02525492

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