[Interaction of frog brain cholinesterase with some reversible ammonium inhibitors].
The effects of some ammonium compounds diiodomethylate acetate (I), propionate (II), butyrate (III), valeriate (IV) N-hydroxyethylanabasine, tetramethylammonium, tetraethylammonium and acetylcholine amide analog derivatives (V-VIII) on acetylthiocholine hydrolysis by cholinesterase from frog brain, acetylcholinesterase from human erythrocytes and butyryl cholinesterase from horse blood serum were studied. Cholinesterase from frog brain possesses a lower sensitivity to the inhibitors than does the mammalian enzyme. Significant conformational changes of the inhibitor molecule, i. e. transition from trans-conformation (V) to the fixed gosh-conformation (VII), have no effect on the anticholinesterase activity of these compounds. A method for evaluation of effectivity of different types of the reversible inhibitors is proposed.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002800:Cholinesterase Inhibitors / Q000494:pharmacology*; D004912:Erythrocytes / Q000201:enzymology; D006736:Horses; D006801:Humans; D007700:Kinetics; D008433:Mathematics; D011896:Rana temporaria; D013329:Structure-Activity Relationship
D002800:Cholinesterase Inhibitors
Vzaimodeĭstvie kholinésterazy mozga liagushki s nekotorymi obratimymi ammonievymi ingibitorami.