Detoxification of cereal plant allelochemicals by aphids: activity and molecular weights of glutathione S-transferase in three species of cereal aphids
1994
Leszczynski, B. | Matok, M. | Dixon, A.F.G.
The activity and molecular weights of glutathione S-transferase were studied in three species of cereal aphid: Metopolophium dirhodum, Sitobion avenae, and Rhopalosiphum padi. The highest level of glutathione S-transferase activity was recorded in extracts from M. dirhodum and the lowest from S. avenae, and extracts of larvae were more active than those from adults. The activity of this enzyme was higher in extracts of S. avenae and R. padi previously fed on a moderately resistant wheat variety than on a susceptible variety. Gel filtration followed by SDS-PAGE revealed three protein bands in the active fractions. The first had a molecular weight of 28,500 and the second of 27,500 and were present in all three species of aphid. The third protein differed in the three species, having a molecular weight of 26.000 in S. avenae, 25,500 in M. dirhodum, and 24,000 in R. padi.
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