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ISOLATION AND PURIFICATION OF CHOLINERGIC RECEPTOR PROTEOLIPIDS FROM RAT GASTROCNEMIUS TISSUE 1

Four organic solvent extraction methods have been used to isolate receptor proteolipids from rat gastrocnemius tissue. The resulting proteolipids have high binding capacities and specificities for a number of cholinergic ligands including acetylcholine, α‐bungarotoxin. tubocurarine and deca‐methonium. The proteolipids have been purified by repeated Sephadex LH‐20, Sepharose‐CL and affinity chromatography in organic solvent systems. Protein, carbohydrate and lipid phosphorous analysis of the receptors throughout the purification procedure show that the relative proportions of these components varied with extraction method. The purified receptor proteolipid resulting from wet tissue extraction has been characterized as a somatic, nicotinic cholinergic receptor by its specificity and binding kinetics toward a variety of drugs and toxins. The presence of carbohydrate in the receptor proteolipid preparations throughout the purification procedure may indicate that the cholinergic receptor from rat gastrocnemius tissue is a glycoproteolipid.