Properties and specificities of a digestive aminopeptidase from larvae of Attagenus megatoma (Coleoptera: dermestidae)

Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae

“…Cathepsin H is an aminopeptidase, activated by thiol compounds, that is usually distinguished by hydrolysis of the specific substrate ArgNA. However, an aminopeptidase isolated from larval midguts of the dermestiid Attagenus megatoma has been shown to hydrolyze several aminoacyl-β-naphthylamides, including ArgNA (Baker and Woo, 1981). We attempted to determine whether ArgNA hydrolysis in the midgut epithelium was due to cathepsin H or aminopeptidases, testing the effects of specific protease inhibitors and activators on the hydrolysis of LpNa and ArgNA by endoperitrophic and midgut epithelium extracts separately.…”

Genetic characterization of the peptidases of Polistes versicolor (Hymenoptera: Vespidae)

“…In this structurally and functionally heterogeneous group, aminopeptidases (EC 3.4.11) are the most electrophoretically studied enzymes in plant and animal species. Among insects, aminopeptidases of Drosophila have been well characterized (Beckman & Johnson, 1964;Sakai et al, 1969;Walker & Williamson, 1980;Walker et al, 1981;Hall, 1986Hall, , 1988, but aminopeptidases from other insects such as the coleopteran Attagenus megatoma (Baker & Woo, 1981), the moth Tineola (Ward, 1975), the dipteran tsétsé fly Glossina (Gooding & Rolselth, 1976), and the lepidopteran Sesamia nonagrioides Lef. (Ortego et al, 1996) have also been studied.…”

Propriedades e secreção das enzimas digestivas e caracterização das membranas microvilares intestinais de insetos

“…A maioria dos trabalhos envolvendo a caracterização de aminopeptidases d insetos realizados até o início da década de 80, utilizaram como fonte de enzima fração solúvel de homogeneizados do intestino médio (Ward, 1975a, b e c;Goodin & Rolseth, 1976;Baker & Woo, 1981, Van der Westhuizen et. al., 1981.…”

“…The R. americana midgut caeca soluble amino peptidases resemble those from other insect source in their broad specificity towards aminoacyl-IJ naphthylamides, in their higher activity on tripeptide rather than on dipeptides, in their inhibition by Tri and phenanthroline and in their low sensitivity to wards EDTA (Ward, 1975a, b;Baker and Woo 1981). Furthermore, the soluble aminopeptidase from R. americana, like those of Tineola bisselliella occur as families of charge variants of what seem t be the same enzyme protein (Ward, 1975a, b).…”

“…Aminopeptidases are usually metallo-enzyme which become inactivated by extensive dialysi against metal chelators such as EDTA (Baker an Woo, 1981). Otherwise, I,IO-phenanthroline (a chela tor weaker than EDTA, cf.…”