Distribution of proteinases and carbohydrases in the midgut of larvae of the sweetpotato weevil Cylas formicarius elegantulus and response of proteinases to inhibitors from sweet potato
1984
Baker, J.E. | Woo, S.M. | Mullen, M.A.
Endoproteinase activity was confined to luminal fluid from anterior and posterior ventricular regions of midguts of larvae of the sweetpotato weevil, Cylas formicarius elegantulus (Summers). Aminopeptidase was found in luminal fluid (18%) but was primarily associated with insoluble fractions from cells of the posterior ventriculus (82%). Depending on substrate, carboxypeptidase activity was about equally distributed between luminal fluid and insoluble fractions from posterior ventriculus cells. Amylase was found in luminal fluid in both the anterior and posterior ventriculus. Five bands of amylase activity were detected on starch zymograms following electrophoresis of whole midgut samples. Three of the amylase bands may be plant-derived. At least two α-glucosidases were present, one secreted and one bound to anterior ventriculus cells. β-Glucosi-dase activity was bound to anterior ventriculus cells whereas α-galactosidase activity was confined to luminal fluid. β-Galactosidase and cellulase activities were found in both luminal fluid and the insoluble cell fraction. Thus, initial digestion of large protein and carbohydrate polymers occurs in luminal fluid in both anterior and posterior ventriculus regions. However, terminal digestion of oligopeptides occurs primarily in the posterior ventriculus while terminal digestion of oligosaccharides occurs in the anterior ventriculus. A 20-fold difference in trypsin-inhibitor concentration was found among five sweetpotato cultivars. Endoproteinases from sweetpotato weevil larvae were inhibited by extracts from the cultivars but cultivars with relatively high concentrations of inhibitor were previously shown to be susceptible to weevil attack in field trials.
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