[Purification of a protein binding quinacrine and histrionicotoxin from membrane fragments rich in cholinergic receptors in Torpedo marmorata].
A protein is purified by differential centrifugation from membrane fragments rich in acetylcholine receptor prepared from Torpedo marmorata electric organ after dissolution by a mixture of non denaturing detergents. After polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate and Coomassie blue staining the purified protein yields a single band of apparent molecular weight 43,000. Spectroscopic experiments carried out in the absence of Ca++ and detergents reveal that the 43 K protein interacts with the fluorescent local anesthetic quinacrine and with the frog toxin histrionicotoxin (apparent KD : 7 X 10(-7) M) but not with carbamylcholine and the alpha toxin from N. nigricollis.
D000109:Acetylcholine / Q000378:metabolism*; D000664:Amphibian Venoms / Q000378:metabolism*; D000818:Animals; D001001:Anura; D001667:Binding, Competitive; D004557:Electric Organ / Q000378:metabolism*; D005399:Fishes; D007700:Kinetics; D008970:Molecular Weight; D011796:Quinacrine / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000302:isolation & purification* / Q000378:metabolism
D000664:Amphibian Venoms; D011950:Receptors, Cholinergic; D011796:Quinacrine; D000109:Acetylcholine
Purification d'une protéine liant la quinacrine et l'histrionicotoxine à partir de fragments de membranes riches en récepteur cholinergique de Torpedo marmorata.