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^ШХР: *http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1570-7458 /issues (по 2010 г. EBSCO) (http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1570-7458/ issues (по 2010 г. EBSCO))
^АВТ: Parde V.D.; Sharma H.C.; Kachole M.S.
^ЗГЛ: Inhibition of Helicoverpa armigera gut pro-proteinase activation in response to synthetic protease inhibitors [Ингибирование активности про-протеиназ средней кишки гусениц хлопковой совки (Helicoverpa armigera) в ответ на обработку синтетическими ингибиторами протеиназ. (Индия)]
^ВЫХ: Entomologia Experimentalis et Applicata, 2012; Vol.142,N 2. - P. 104-113
^ДАТ: 2012
^ПРМ: Режим доступа:http://search.epnet.com.- Bibliogr.:p.112-113
+Реферат:

^РЕФ: Protease inhibitors play an important role in host plant defence against herbivores. However, insects have the ability to elevate the production of proteinases or resort to production of a diverse array of proteinases to offset the effect of proteinase inhibitors. Therefore, we studied the inhibition of pro-proteinase(s) activation in the midgut of the polyphagous pest Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae) in response to protease inhibitors to develop appropriate strategies for the control of this pest. Gelatin coating present on X-ray film was used as a substrate to detect electrophoretically separated pro-proteinases and proteinases of H. armigera gut extract on native- and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Six activated pro-proteinase bands were detected in H. armigera gut lumen, which were partially purified and characterized using substrate assays. Activated H. armigera midgut pro-proteinase(s) showed activity maxima at pH 8 and 10, and exhibited optimal activity at 40 °C. The activation of H. armigera gut pro-proteinase isoforms was observed in the fraction eluted on benzamidine-sepharose 4B column. Purification and substrate assay studies revealed that 23-70 kDa polypeptides were likely the trypsin/chymotrypsin-like pro-proteinases. Larvae of H. armigera fed on a cocktail of synthetic inhibitors (antipain, aprotinin, leupeptin, and pefabloc) showed maximum activation of pro-proteinases compared with the larvae fed on individual inhibitors. The implications of these results for developing plants expressing proteinase inhibitors for conferring resistance to H. armigera are discussed. aref1

^TRN: 1568787
^ВИД: Статья из книги
^ЯЗК: Английский
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