An ESR study of the postsynatpic membrane acetylcholinesterase of Torpedo marmorata electric organ.
The effect of the cholinergic activator, phenyltrimethylammonium, on the ESR spectra of spin-labeled membrane bound acetylcholinesterase was studied; a reduction of maximal hyperfine splitting of the anisotropic ESR spectrum by 2 G was observed. The influence of phenyltrimethylammonium was prevented by the two cholinergic blocking agents d-tubocurarine and alpha-cobratoxine. The present results indicate that the conformation change of the esteratic site of membrane acetylcholinesterase is triggered by the binding of phenyltrimethylammonium to the cholinoreceptor site.
D000110:Acetylcholinesterase / Q000378:metabolism; D000494:Allosteric Regulation; D000818:Animals; D004557:Electric Organ / Q000201:enzymology / Q000648:ultrastructure*; D004578:Electron Spin Resonance Spectroscopy; D005260:Female; D005399:Fishes; D008297:Male; D010277:Parasympathomimetics / Q000378:metabolism; D011487:Protein Conformation; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D011978:Receptors, Nicotinic / Q000378:metabolism; D012910:Snake Venoms / Q000494:pharmacology; D013570:Synaptic Membranes / Q000201:enzymology*; D014403:Tubocurarine / Q000494:pharmacology
D010277:Parasympathomimetics; D000644:Quaternary Ammonium Compounds; D011978:Receptors, Nicotinic; D012910:Snake Venoms; D000110:Acetylcholinesterase; D014403:Tubocurarine