title: [Studying kinetics of oxime-induced reactivation of malathion-inhibited cholinesterase].
abstract: The kinetics of oxime-induced reactivation of malathion-inhibited cholinesterase has been experimentally studied in vitro. It is shown that oximes do not restore the activity of inhibited butyrylcholinesterase. Acetylcholinesterase reactivation peak (5-mins long) was found to take place upon introduction of dipyroxime (32.5%), pralidoxime (18%), carboxyme (16%) at a concentration of 2.5 x 10(-4) mol/l or toxogonine (26%) at a concentration of 5 x 10(-4) mol/l. Toxogonine demonstrated the maximum affinity to phosphorylated enzyme, while dipyroxime is characterized by a high reactivity with respect to oxime. Significant reactivating ability of these preparations (kR -2300 mol(-1) min(-1) makes them promising solution for the treatment of malathion intoxication.
authors: M A
authors: MA
authors: Iudin
authors: D V
authors: DV
authors: Lantukhov
authors: N G
authors: NG
authors: Vengerovich
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry*; D000818:Animals; D000931:Antidotes / Q000737:chemistry*; D002091:Butyrylcholinesterase / Q000737:chemistry*; D002800:Cholinesterase Inhibitors / Q000737:chemistry*; D002801:Cholinesterase Reactivators / Q000737:chemistry*; D004789:Enzyme Activation; D004912:Erythrocytes / Q000737:chemistry / Q000201:enzymology; D006736:Horses; D007700:Kinetics; D008294:Malathion / Q000737:chemistry*; D009768:Obidoxime Chloride / Q000737:chemistry; D011220:Pralidoxime Compounds / Q000737:chemistry; D012996:Solutions; D014101:Torpedo; D014289:Trimedoxime / Q000737:chemistry
chemical_list: D000931:Antidotes; D002800:Cholinesterase Inhibitors; D002801:Cholinesterase Reactivators; D011220:Pralidoxime Compounds; D012996:Solutions; D009768:Obidoxime Chloride; D014289:Trimedoxime; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase; C028797:pralidoxime; D008294:Malathion