Acetylcholine binding to Torpedo electroplax: relationship to acetylcholine receptors.
Binding of [(3)H]acetylcholine to a particulate fraction of Torpedo electroplax was measured by equilibrium dialysis. Two high-affinity sites present on phospholipoproteins bound acetylcholine reversibly, and binding was blocked by nicotinic drugs. Characteristics of this binding suggest that these phospholipoproteins may be acetylcholine receptors.
D000109:Acetylcholine / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D003650:Decamethonium Compounds / Q000378:metabolism; D003956:Dialysis; D004524:Eels; D004557:Electric Organ / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects; D008074:Lipoproteins / Q000378:metabolism; D046911:Macromolecular Substances; D009539:Nicotinic Acids / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D011950:Receptors, Cholinergic; D011955:Receptors, Drug; D014403:Tubocurarine / Q000378:metabolism
D003650:Decamethonium Compounds; D008074:Lipoproteins; D046911:Macromolecular Substances; D009539:Nicotinic Acids; D011950:Receptors, Cholinergic; D011955:Receptors, Drug; D000109:Acetylcholine; D014403:Tubocurarine