Malathion toxicity and carboxylesterase activity in Drosophila melanogaster
Pesticide Biochemistry and Physiology, ISSN: 0048-3575, Vol: 29, Issue: 2, Page: 97-111
1987
- 19Citations
- 10Captures
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Article Description
Adults from nine strains of Drosophila melanogaster were exposed to a residual film of malathion. The LC 50 values indicated that there was a fourfold difference in susceptibility to malathion among the strains. 3-Nonylthio-1,1,1-trifluoropropan-2-one (NTFP), a carboxylesterase inhibitor, synergized the toxicity of the insecticide when four fly strains were exposed to a mixture of the inhibitor and malathion. Whole-body homogenates of adults were analyzed by wide-range isoelectric focusing (IEF). Carboxylesterase activities on the gels were stained using common substrates such as α- and β-naphthyl acetate and p -nitrophenyl acetate. Less conventional substrates, ethyl and isobutyl carbonates of α-naphthol and p -nitrophenol, were synthesized and used for staining gels and kinetics in solution. Two major bands of activity (p I 4.4 and 4.0) were detected with naphthyl substrates. A major peak of malathion hydrolytic activity (p I 6.3) was detected by running spectrophotometric assays for carboxylesterase activity on malathion using IEF gel slices and a rapid, semiautomated assay method. The peak region of activity on malathion did not coincide with bands obtained when naphthyl substrates were used to stain the gels. NTFP inhibited malathion hydrolysis in a solution from the IEF peak of activity and also inhibited esterase activity on α-naphthyl acetate on the gels. Recovered carboxylesterase activities on malathion and O -ethyl carbonate of p -nitrophenol were higher in the cytosolic than in the microsomal or mitochondrial cell fractions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0048357587900678; http://dx.doi.org/10.1016/0048-3575(87)90067-8; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0023551241&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/0048357587900678; https://api.elsevier.com/content/article/PII:0048357587900678?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:0048357587900678?httpAccept=text/plain; http://dx.doi.org/10.1016/0048-3575%2887%2990067-8; https://dx.doi.org/10.1016/0048-3575%2887%2990067-8
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