Abstract
The nicotinic acetylcholinergic receptor has been isolated and purified from extracts of the electric organ of the fish Torpedo fascomaculata. The isolation procedure involves (a) a series of purification steps including preparation of membrane fragments, extraction of receptors with non-ionic detergents and chromatofocusing; (b) a novel fluorimetric titration assay. The purified receptor is isolated following a 9-fold purificaton with an overall yield of 12% and a specific activity of 4027 nM · g −1. Gel electrophoresis in the presence of sodium dodecysulphate produced only one major brand with molecular weight of 44 600 associated with the α-subunit. A comparison is made with other established procedures. Affinity chromatography on cobratoxin CNBr-Sepharose CL4B produced a 6.8-fold purification, 5% yield and 2900 nM · g −1 specific activity, while in ion-exchange chromatography on DEAE Sepharose 6B gave a 4.7-fold purificatiom, 3% yield and specific activity of 1988 nM · g −1.
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