Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4348
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dc.contributor.authorAurade R.M
dc.contributor.authorJayalakshmi S.K
dc.contributor.authorUdikeri S.S
dc.contributor.authorSreeramulu K.
dc.date.accessioned2020-06-12T15:03:39Z-
dc.date.available2020-06-12T15:03:39Z-
dc.date.issued2012
dc.identifier.citationArchives of Insect Biochemistry and Physiology , Vol. 79 , 1 , p. 47 - 60en_US
dc.identifier.uri10.1002/arch.21004
dc.identifier.urihttp://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4348-
dc.description.abstractPurified P-glycoprotein ATPase from Helicoverpa armigera (Ha-Pgp), reconstituted in proteoliposomes composed of phospholipids and cholesterol, shows higher ATPase activity in the presence of cholesterol than in its absence. The Ha-Pgp ATPase activity was increased 30-40% with cholesterol. The KM for ATP was found to be 1 and 0.8 mM in the absence and presence of cholesterol, respectively. The insecticide-stimulated Ha-Pgp ATPase activity was increased by 10-20% for all the insecticides in the reconstituted proteoliposomes containing cholesterol compared to those with no cholesterol. The effects of cholesterol on KM and Vmax values of insecticide-stimulated Ha-Pgp ATPase activity were unrelated to the size of the insecticide. Ha-Pgp tryptophan fluorescence displayed a red shift of 3 and 8 nm in emission spectra upon binding of insecticides. Cholesterol enhances the interaction of insecticides with Ha-Pgp. Kd values of different insecticides for binding to Ha-Pgp were found to be lower in the presence of cholesterol in the proteoliposomes compared to its absence. Results suggest that cholesterol plays a role in the recognition and interaction of insecticides by modulating Ha-Pgp ATPase and may be involved in efflux of insecticides from cells by the transporter. © 2011 Wiley Periodicals, Inc.en_US
dc.subjectCholesterol
dc.subjectHelicoverpa armigera
dc.subjectInsecticides
dc.subjectP-glycoprotein atpase
dc.subjectTryptophan quenching
dc.titleModulation of P-glycoprotein atpase of helicoverpa armigera by cholesterol: Effects on atpase activity and interaction of insecticidesen_US
dc.typeArticle
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