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Tomas Erban,Jitka Stara 한국응용곤충학회 2014 Journal of Asia-Pacific Entomology Vol.17 No.3
Glutathione S-transferases (GSTs) are one of the major detoxification enzymes involved in insecticide resistance. In this study, optimized methodology for GSTs purification and localization in two-dimensional gel electrophoresisis shown on the pollen beetle. Specifically, the GST proteins were purified using GSTrap 4B column, andthe protein profile of the supernatant before purification was compared with the unbound fraction postpurificationvia two-dimensional gel electrophoresis (2D-E). The identity of these localized protein spots wasconfirmed by MS analysis and further analyzed by NanoLC-ESI-QUAD-TOF-MS/MS protein identification. Resultsindicate that 2 out of 5 protein spots were GSTswith region for class Delta and Epsilon subfamilies similar to otherinsects; however, the remaining 3 spots did not show any match in the current NCBInr. Both Delta and Epsilonclass GSTs are specifically involved in insecticide resistance and their relatively high abundance in the 2D-Emap suggests that these enzymes could play a role in the resistance of Meligethes aeneus to the most commonlyused pyrethroids. The approach applied in this study for the specific localization of GSTs in 2D-E can be used forsimilar analyses in other organisms.