ORGANOPHOSPHATE INHIBITION OF NEMATODE ESTERASES AND INTERACTION WITH CHLORINATED HYDROCARBON INSECTICIDES By
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منابع مشابه
Fitness costs of insecticide resistance in natural breeding sites of the mosquito Culex pipiens.
Genetic changes conferring adaptation to a new environment may induce a fitness cost in the previous environment. Although this prediction has been verified in laboratory conditions, few studies have tried to document this cost directly in natural populations. Here, we evaluated the pleiotropic effects of insecticide resistance on putative fitness components of the mosquito Culex pipiens. Exper...
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Culex tritaeniorhynchus Giles and Cx. gelidus Theobald (Diptera: Culicidae), both vectors of Japanese encephalitis, were collected in 1984 and 1998 from two disease endemic localities in Sri Lanka: Anaradhapura and Kandy. Using wild-caught adult mosquitoes from light traps, log dosage-probit mortality curves for insecticide bioassays were obtained for three insecticides: malathion (organophosph...
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Organophosphates are organic substances that contain a phosphoryl or a thiophosphoryl bond. They are mainly used around the world as pesticides, but can also be used as chemical warfare agents. Their detection is normally entrusted to techniques like GC- and LC-MS that, although sensitive, do not allow their identification on site and in real time. We have approached their identification by exp...
متن کاملCharacterization of a B-type esterase involved in insecticide resistance from the mosquito Culex quinquefasciatus.
The enzyme, esterase B2, involved in insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has an M(r) of 62000 and a pI of 5.0. This enzyme is compared with the esterase A2 previously characterized [Ketterman, Jayawardena and Hemingway (1992) Biochem. J. 287, 355-360]. The kinetic constants for interaction with several insecti...
متن کاملInhibition of “Serine” Esterases by Phenylarsonic Acids
Chymotrypsin, trypsin, and Novo and Carlsberg subtilisins undergo a reversible, time-dependent inhibition by phenylarsonates. The inhibition of these enzymes by p-nitro-, p-tolyl-, p-aminophenyl-, and phenylarsonate was studied in detail, as a function of pH and inhibitor concentration, by a variety of approaches. KI values were determined for the inhibition of chymotrypsin and the subtilisins ...
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تاریخ انتشار 2008