Differentiation of glycosidase activity in some Hemiptera and Lepidoptera by means of castanospermine and other polyhydroxy alkaloids
1995
Scofield, A.M. | Witham, P. | Nash, R.J. | Kite, G.C. | Fellows, L.E.
Inhibition of glycosidase activity by a range of polyhydroxy alkaloids was studied in a number of insect species. Castanosperimine, usually inactive against maltose and sucrose hydrolysis in insects, was an active inhibitor of maltose hydrolysis in aphids and Heliconius melpomone at pH5.1 but inactive at pH 6.0. Conversely, 2R.5R-dihydroxymethyl-3R,4R-ddhydroxypyrrolidine, normally a potent inhibitor of insect sucrose and maltose hydrolysis, was relatively ineffective in the former species at pH 5.1. The data suggest that several separate enzymes or active sites were responsible for maltose and sucrose hydrolysis in aphids and H. melpomone.
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