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CATHEPSIN B AND AMINOPEPTIDASE ACTIVITY IN THE POSTERIOR MIDGUT OF EUSCHISTUS EUSCHISTOIDES (HEMIPTERA: PENTATOMIDAE)

Published online by Cambridge University Press:  31 May 2012

Jon G. Houseman ,
W. K. MacNaughton  and
A. E. R. Downe
Jon G. Houseman
Affiliation:
Department of Biology, Queen's University, Kingston, Ontario K7L 3N6
W. K. MacNaughton
Affiliation:
Department of Biology, Queen's University, Kingston, Ontario K7L 3N6
A. E. R. Downe
Affiliation:
Department of Biology, Queen's University, Kingston, Ontario K7L 3N6
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Abstract

The posterior midgut of a seed-feeding pentatomid, Euschistus euschistoides (Vollenhoven), contains the proteinases cathepsin B and aminopeptidase. Cadiepsin B hydrolysis of benzoyl-DL-arginine-2-naphthylamide is activated by thiol chemicals and EDTA. Aminopeptidase hydrolysis of leucine-p-nitroanilide is activated by MgCl2 and inhibited by cysteine, glutathione, EDTA, and CaCl2. These results are similar to those obtained for cathepsin B and aminopeptidase from blood-feeding Hemiptera and support the hypothesis that catheptic proteinases are unique to this order.

Résumé

Le mésentéron postérieur du pentatomide granivore Euschistus euschistoides (Vollenhoven) contient les proteinases cathepsine B et l'aminopeptidase. L'hydrolyse du ben-zoyl-DL-arginine-2-naphthylamide par la cathepsine B est activée par les produits de type thiol et par l'EDTA. L'hydrolyse de la leucine-p-nitroanilide par l'aminopeptidase est activée par le MgCl2 et inhibée par la cysteine, le glutathione, l'EDTA et le CaCl2. Ces résultats sont semblables à ceux obtenus avec la cathepsine B et l'aminopeptidase provenant d'hémiptères hématophages, appuyant l'hypothèse voulant que les proteinases catheptiques sont uniques à cet ordre.

Type
Articles
Information
The Canadian Entomologist , Volume 116 , Issue 10 , October 1984 , pp. 1393 - 1396
Copyright
Copyright © Entomological Society of Canada 1984

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