[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.
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