[Anticholinesterase properties and metabolism of new thiophosphonates with a carboxy ester bond in the phosphoryl portion of the molecule].
Introduction of the carboxyester bond into the phosphoryl part of thiophosphonate molecules did not affect their capacity to inhibit cholinesterases, but increased the rate of enzymatic detoxication of the preparations. The enzymatic turnover of the drugs studied occurred in rat tissues mainly be means of hydrolysis of the complex-ester bond. The carboxyesterase hydrolysis of these drugs was apparently carried out involving the unspecific enzyme aliesterase (EC 3.1.1.1.).
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000378:metabolism*; D006736:Horses; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D063086:Organothiophosphates / Q000378:metabolism / Q000494:pharmacology*; D009946:Organothiophosphorus Compounds / Q000494:pharmacology*; D051381:Rats; D013329:Structure-Activity Relationship; D014018:Tissue Distribution
D002800:Cholinesterase Inhibitors; D063086:Organothiophosphates; D009946:Organothiophosphorus Compounds; D002265:Carboxylic Ester Hydrolases
Antikholinesteraznye svoĭstva i metabolizm novykh tiofosfonatov s karboksiéfirnoĭ sviaz'iu v fosforil'noĭ chasti molekuly.