The activity and molecular weights of glutathioneS-transferase were studied in three species of cereal aphid:Metopolophium dirhodum, Sitobion avenae, andRhopalosiphum padi. The highest level of glutathioneS-transferase activity was recorded in extracts fromM. dirhodum and the lowest fromS. avenae, and extracts of larvae were more active than those from adults. The activity of this enzyme was higher in extracts ofS. avenae andR. 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 inS. avenae, 25,500 inM. dirhodum, and 24,000 inR. padi.