Cholinesterase inhibition in the bulb miteRhizoglyphus echinopus (Acari: Acaridae) in relation to the acaricidal action of organophosphates and carbamates

The 5000-g supernatant fraction of whole-bulb-mite homogenates was shown to possess a cholinesterase (ChE) that hydrolyzed acylcholine esters in the order acetyl>propionyl>butyryl. Acetyl--methylcholine, but not benzoylcholine, also was hydrolyzed as were acetylthiocholine and acetyl--methylthiocholine. No inhibition by excess substrate was observed at cholinester concentrations as high as 30mM. Cholinesterase activity was markedly insensitive to eserine and to certain other carbamates and organophosphates. Only organophosphates of the dimethylphosphate type generally were active ChE inhibitors. It was concluded that the inability of carbamates such as eserine, and organophosphates such as those with alkyl groups larger than dimethyl, to inhibit the bulb-mite ChE was probably a consequence of the nature of the esteratic site. The data suggested that ChE inhibition was likely involved in the toxicity to bulb mites of some of the toxic carbamates and organophosphates, but that it might not be the only mechanism involved, at least with several of the compounds.Contribution from the Missouri Agricultural Experiment Station, Columbia, MO, Journal Series No. 10 924.