Proteolytic gut activities in the rice water weevil, Lissorhoptrus brevirostris suffrian (Coleoptera: curculionidae)

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 th...

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Bibliographic Details
Published in:Archives of insect biochemistry and physiology 2003-05, Vol.53 (1), p.19-29
Main Authors: Hernandez, C.A, Pujol, M, Alfonso-Rubi, J, Armas, R, Coll, Y, Perez, M, Gonzalez, A, Ruiz, M, Castanera, P, Ortego, F
Format: Article
Language:English
Subjects:
Animals
cathepsins
chymotrypsin
Coleoptera - enzymology
Curculionidae
Cysteine - pharmacology
digestion
digestive enzymes
Digestive System - anatomy & histology
Digestive System - enzymology
digestive tract
Dithiothreitol - pharmacology
Electrophoresis, Polyacrylamide Gel - methods
Endopeptidases - metabolism
endoprotease
Enzyme Activation
enzyme activity
Enzyme Inhibitors - pharmacology
Freshwater
Hydrogen-Ion Concentration
insect pests
Larva
Lissorhoptrus
Lissorhoptrus brevirostris
protease inhibitors
Protease Inhibitors - pharmacology
proteases
proteinase inhibitors
proteinases
proteolysis
rice water weevil
spatial distribution
Substrate Specificity
trypsin
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Summary: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. Arch. Insect Biochem. Physiol. 53:19–29, 2003. © 2003 Wiley‐Liss, Inc.
ISSN:0739-4462
1520-6327
DOI:10.1002/arch.10083