Biochemistry of Esterases Associated with Organophosphate Resistance in Lucilia cuprina with Comparisons to Putative Orthologues in Other Diptera：（生物化学与有机磷抗性相关的酯酶在Lucilia cuprina与比较公认的Orthologues其他双翅目）.pdfVIP

Biochemical Genetics, Vol. 35, Nos. 1/2, 1997 Biochemistry of Esterases Associated with Organophosphate Resistance in Lucilia cuprina with Comparisons to Putative Orthologues in Other Diptera Peter M. Campbell,1,2 Josephine F. Trott,3,4 Charles Claudianos,1 1,5 1 1 Kerrie-Ann Smyth, Robyn J. Russell, and John G. Oakeshott Received 16 Oct. 1996—Final 21 Jan. 1997 Esterase activities associated with organophosphate insecticide resistance in the Australian sheep blowfly, Lucilia cuprina , are compared with similar activities in other Diptera. The enzymes making the major contribution to methyl butyrate hydrolysis {ali-esterase) in L. cuprina , M. domestica, and D. melanogaster comigrate during electrophoresis. The enzymes in L. cuprina and D. melanogaster correspond to the naphthyl acetate hydrolyzing E3 and EST23 isozymes of those species. These and previously published data suggest that the ali-esterases of all three species are orthologous. Strains of L. cuprina fall into four groups on the basis of quantitative determinations of their ali-estesterase, OP hydrolase, and malathion carboxylesterase activities and these groups correspond to their status with respect to two types of OP resistance. Strains susceptible to OPs have high ali-esterase, low OP hydrolase, and intermediate MCE activities; those resistant to malathion but not diazinon have low ali-esterase, intermediate OP hydrolase, and high MCE activities; those resistant to diazinon but not malathion have low ali-esterase, high OP hydrolase, and low MCE activities; those resistant to