Sobel A, Heidmann T, Changeux J P
C R Acad Hebd Seances Acad Sci D. 1977 Nov 21;285(14):1255-8.
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.
用非变性去污剂混合物溶解电鳐电器官制备的富含乙酰胆碱受体的膜碎片，通过差速离心法纯化一种蛋白质。在十二烷基硫酸钠存在下进行聚丙烯酰胺凝胶电泳并经考马斯亮蓝染色后，纯化的蛋白质产生一条表观分子量为43,000的单带。在不存在钙离子和去污剂的情况下进行的光谱实验表明，43K蛋白与荧光局麻药喹吖因以及青蛙毒素组氨酸毒素相互作用（表观解离常数KD：7×10^(-7) M），但不与氨甲酰胆碱和黑颈眼镜蛇的α毒素相互作用。
