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- W879487211 abstract "[ ]Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, -glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose, sucrose, trehalose, and p-nitrophenyl -D-glucopyranoside as substrates. In general, hemolymph -glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut -glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. -Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl -D-glucoside (MUG) indicated that the -glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to -glucosidase activity from A. yamamai, -glucosidase activity from B. mori was generally less sensitive to the -glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose, sucrose, and trehalose." @default.
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- W879487211 date "2010-01-01" @default.
- W879487211 modified "2023-09-28" @default.
- W879487211 title "Comparative Analysis of $alpha$ -glucosidase Activity in Bombyx mori and Antheraea yamamai" @default.
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