Add time:08/25/2019         Source:sciencedirect.com

A series of branched-chain analogs of diethyl malathion and malaoxon were prepared in which the “leaving group” consisted of either malonate, succinate, α-glutarate, or β-glutarate diethyl esters. The single-dose oral toxicities of these compounds as determined for female Duplin white mice showed the α-glutarate analogs to be the most toxic and the β-glutarate analogs the least toxic. Inhibiting carboxylesterase in vivo with tri-o-tolyl phosphate (TOCP) demonstrated that all the compounds were substrates for carboxylesterase. The house fly LD50 data showed the β-glutarate analogs to be the least toxic in the series.In vitro studies with rat liver carboxylesterase and the branched-chain analogs of diethyl malathion also demonstrated that all the compounds were hydrolyzed by liver carboxylesterase. The inhibition studies showed the malonate malaoxon was the most active inhibitor to cholinesterase and carboxylesterase. No overall correlation between toxicity and in vitro enzymatic activity was found.

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