[Enzymatic transformation of O-heptyl-O-orthonitrophenylmethylphosphonate--a cholinesterase--blocking agent in rat tissue homogenates].
The study of enzymic transformations of O-heptyl-O-orthonitrophenylmethylphosphate in homogenates in the liver, kidney, brain and in blood serum of rats revealed the hydrolysis of aryl-phosphate bound only. Certain data are obtained illustrating identity of the enzyme under study to paraoxonase. The results of the experiments showed that IP-optical isomers of O-heptyl-O-orthonitrophenylphosphonate are likely to exist, the hepatic and renal enzymes possessing the pronounced stereospecificity and destroying preferably the dextrorotatory isomer.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002800:Cholinesterase Inhibitors / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D009943:Organophosphorus Compounds / Q000378:metabolism*; D051381:Rats; D013237:Stereoisomerism
D002800:Cholinesterase Inhibitors; D009943:Organophosphorus Compounds