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Purification of Acetylcholine Receptor‐like Protein from Fetal Calf Thymus

Abstract: A cobrotoxin binding protein from the fetal calf thymus was isolated by affinity chromatography after solubilization with sodium cholate. The specific activity as a nicotinic acetylcholine receptor (AChR) was determined by assessing the bindingto [3H]‐α‐bungarotoxin (BuTx), using the high‐pressure liquid chromatography. An AChR‐like protein was detected in the amount of 1.39–2.14 nmol per g protein. The first peak of 420k‐protein from gel filtration of the eluate of affinity chromatography on aSephacryl column showed one major polypeptide band with an Mr of 40k, by polyacrylamide gel electrophoresis in sodium dodecylsulfate, two major protein bands with pi 5.4–5.6 and9.2 by isoelectric focusing, and reacted with sera from patients with myasthenia gravis.