Isolation of a putative nicotinic acetylcholine receptor from the central nervous system of Locusta migratoria.

The alpha-bungarotoxin binding component from locust central nervous tissue was solubilized and purified by affinity chromatography on alpha-bungarotoxin Sepharose 4B. On sucrose density gradients containing Triton X-100, the toxin binding site sedimented with an apparent sedimentation coefficient of about 10 S. As revealed by sodium dodecylsulfate polyacrylamide gel electrophoresis, the purified receptor protein was composed predominantly of 65,000 molecular weight polypeptides.