title: Biochemical studies on the ionic channel of Torpedo acetylcholine receptor.
abstract: 1. [3H]H12-HTX binding to Torpedo electric organ membranes is saturable and inhibited by ligands that modulate EPCs. There is a small proportion of nonspecific binding to the membrane. 2. The validity of utilizing [3H]H12-HTX as a specific label for the ionic channel of the nicotinic receptor is extablished by the good correlation between the potency of HTX analogues in reducing EPC amplitudes and their inhibition of [3H]H12-HTX binding. 3. Receptor drugs and toxins inhibit [3H]ACh binding to the ACh receptor, but do not inhibit significantly [3h]h12-htx binding to the ionic channel at similar concentrations. 4. Various drugs and toxins with different modes of action modulate EPCs and inhibit [3H]H12-HTX binding to the ionic channel of the nicotinic receptor. Most such drugs and toxins, at similar concentrations, do not inhibit [3H]ACh binding to the ACh receptor, but some do, such as quinacrine and TEA. 5. The ionic channel of the nicotinic receptor is a protein which is solubilized by cholate and retains its affinity for H12-HTX as well as its drug sensitivity. 6. The ACh receptor is separated from its ionic channel, and different conditions affect the proportion of separated molecules.
mesh_terms: D000109:Acetylcholine / Q000378:metabolism*; D000664:Amphibian Venoms / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D005399:Fishes; D007473:Ion Channels / Q000032:analysis*; D008566:Membranes / Q000502:physiology; D010880:Piperidines / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000302:isolation & purification; D011978:Receptors, Nicotinic / Q000378:metabolism; D012964:Sodium / Q000378:metabolism; D012995:Solubility
chemical_list: D000664:Amphibian Venoms; D007473:Ion Channels; D010880:Piperidines; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic; D012964:Sodium; D000109:Acetylcholine