Hernández, C.A. and Pujol, M. and Alfonso-Rubí, J. and et al, . (2003) Proteolytic gut activities in the rice water weevil, Lissorhoptrus brevirostris Suffrian (Coleoptera: Curculionidae). Archives of Insect Biochemistry and Physiology, 53 (1). pp. 19-29.
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Abstract
Digestive endoprotease activities of the rice water weevil, Lissorhoptrus brevirostris Suffrian (Coleoptera: Curculionidae), were characterized based on the ability of gut extracts to hydrolyze specific synthetic substrates, optimal pH, and hydrolysis sensitivity to protease inhibitors. Larvae of this species were found to use a complex proteolytic system that includes cathepsin D-, cathepsin B-, trypsin-, and chymotrypsin-like activities. Trypsin-like activity was evenly distributed among the anterior, middle, and posterior portions of the gut, whereas cathepsin B– and cathepsin D–like activities were mainly located in the anterior and middle sections, and the chymotrypsin-like activity was highest in the middle and posterior sections. Gelatin-containing native-PAGE gels indicated the presence of several aspartyl, cysteine, and serine protease forms and confirmed the spatial organization of the proteolytic digestive process
Item Type: | Article |
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Uncontrolled Keywords: | Lissorhoptrus brevirostris; Rice water weevil; Proteases; Protease inhibitors |
Author Affiliation: | Center for Genetic Engineering and Biotechnology, Sancti Spiritus, Cuba |
Subjects: | Plant Protection Plant Physiology and Biochemistry > Plant Physiology Plant Physiology and Biochemistry > Biochemistry |
Divisions: | General |
Depositing User: | Ms Ishrath Durafsha |
Date Deposited: | 12 Aug 2015 04:57 |
Last Modified: | 12 Aug 2015 04:57 |
Official URL: | http://dx.doi.org/10.1002/arch.10083 |
URI: | http://eprints.icrisat.ac.in/id/eprint/13350 |
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