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Titolo:
BIOCHEMISTRY OF ESTERASES ASSOCIATED WITH ORGANOPHOSPHATE RESISTANCE IN LUCILIA-CUPRINA WITH COMPARISONS TO PUTATIVE ORTHOLOGUES IN OTHER DIPTERA
Autore:
CAMPBELL PM; TROTT JF; CLAUDIANOS C; SMYTH KA; RUSSELL RJ; OAKESHOTT JG;
Indirizzi:
CSIRO,DIV ENTOMOL,POB 1700 CANBERRA ACT 2601 AUSTRALIA UNIV SYDNEY,DEPT ANIM SCI,FAC AGR SYDNEY NSW 2006 AUSTRALIA
Titolo Testata:
Biochemical genetics
fascicolo: 1-2, volume: 35, anno: 1997,
pagine: 17 - 40
SICI:
0006-2928(1997)35:1-2<17:BOEAWO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCA-DOMESTICA L; ORGANO-PHOSPHORUS INSECTICIDES; DROSOPHILA-MELANOGASTER; WIEDEMANN DIPTERA; GENETIC MAPS; MALATHION; CALLIPHORIDAE; CARBOXYLESTERASE; ISOMALATHION; DIAZINON;
Keywords:
ORGANOPHOSPHORUS INSECTICIDE RESISTANCE; ESTERASE; LUCILIA CUPRINA; MUSCA DOMESTICA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
P.M. Campbell et al., "BIOCHEMISTRY OF ESTERASES ASSOCIATED WITH ORGANOPHOSPHATE RESISTANCE IN LUCILIA-CUPRINA WITH COMPARISONS TO PUTATIVE ORTHOLOGUES IN OTHER DIPTERA", Biochemical genetics, 35(1-2), 1997, pp. 17-40

Abstract

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 bow 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 both OPs have low ali-esterase, high OP hydrolase, and high MCE activities. The correlated changes among the three biochemical and two resistance phenotypes suggest that they are all properties of one gene/enzyme system; three major allelic variants of that system explain OP susceptibility and the two types of OP resistance. Models are proposed to explain the joint contribution of OP hydrolase and MCE activities to malathion resistance and the invariant association of low ali-esterase and elevated OP hydrolase activities in either type of resistance.

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Documento generato il 08/08/20 alle ore 09:00:37