Abstract
The rates at which several diarylhaloethanes structurally related to DDT were enzymatically dehydrohalogenated by homogenates of DDT-susceptible and DDT-resistant house flies ( Musca domestica L.) were determined. Diarylbromoethanes were dehydrohalogenated much more readily than similar chlorinated compounds. DDT-susceptible flies exhibited considerable dehydrobrominase activity, possibly sufficient to account for the low toxicity of the bromine analogs of DDT to the insects. No evidence of enzymatic preference for either enantiomorph of a racemic mixture of an optically active substrate was found.
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