Chemical Properties of Quinol Phosphate Esters and Inhibition of Alcohol Dehydrogenase by Them
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Eto et al. as mentioned in this paper found that quinol phosphates are susceptible to oxidation and inhibit the SH-enzyme alcohol dehydrogenase, which has been known as a malathion synergist.Abstract:
In a previous paper (Eto et al., 1975), we found the metabolic formation of a quinol phosphate in houseflies from triphenyl phosphate, which has been known as a malathion synergist (Plapp et al., 1963). It has been also reported that the fungicide edifenphos (S, S-diphenyl ethyl phosphorodithiolate ; HinosanQ) was partially metabolized through p-hydroxylation in Pyricularia oryzae (Uesugi and Tomizawa, 1971). Quinol phosphates are known to be activated oxidatively (Blackburn and Cohen, 1968). By oxidation, a quinol phosphate will give a quinone which may react with SH-compounds. This paper describes that quinol phosphates are susceptible to oxidation and inhibit the SH-enzyme alcohol dehydrogenase.read more
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Tissue sulfhydryl groups
TL;DR: A water-soluble (at pH 8) aromatic disulfide [5,5′-dithiobis(2-nitrobenzoic acid] has been synthesized and shown to be useful for determination of sulfhydryl groups.
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[79] Alcohol dehydrogenase from baker's yeast: RCH2OH + DPN+ ⇄ RCHO + DPNH + H+
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Synergism of malathion against resistant house flies and mosquitoes.
TL;DR: It was considered that the synergists worked by blocking the increased ability of resistant insects to degrade either malathion or its oxygen analog, malaoxon, and provided evidence that with eertain synergists resistance to organophosphate insecticides could be overcome by inhibition of degradation mechanisms.
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