[Interaction of membrane-bound and solubilized acetylcholinesterase from human and bovine erythrocytes with organophosphorus inhibitors].
Differences are found between the membrane-bound and soluble acetylcholinesterases of human and bovine erythrocytes when the enzyme interacts with organophosphoric inhibitors in the presence of acetylc choline and galantamine, a reverse inhibitor of acetylcholinesterase. In most cases prevention of inhibition of the soluble enzyme activity necessitates a higher (2-3 times higher) concentration of the protecting agent than protection of the membrane-bound enzyme. Concentrations of acetylcholine and galantamine providing a 50% protection of the enzyme did not practically depend on the strength of the anticholinesterase action of organophosphoric inhibitors.
D000110:Acetylcholinesterase / Q000097:blood*; D000818:Animals; D002417:Cattle; D002800:Cholinesterase Inhibitors / Q000378:metabolism*; D002801:Cholinesterase Reactivators / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D009943:Organophosphorus Compounds / Q000378:metabolism*; D012995:Solubility; D013045:Species Specificity; D013329:Structure-Activity Relationship
D002800:Cholinesterase Inhibitors; D002801:Cholinesterase Reactivators; D009943:Organophosphorus Compounds; D000110:Acetylcholinesterase
Vzaimodeĭstvie membranosviazannoĭ i soliubilizirovannoĭ atsetilkholinésterazy éritrotsitov cheloveka i byka s fosfororganicheskimi ingibitorami.