Kawanami_1988_J.Neurol.Sci_87_195

A nicotinic acetylcholine receptor-like protein (AChR-LP) was isolated from fetal calf thymus by affinity chromatography using cobrotoxin-Sepharose after alkaline extraction and solubilization with Triton X-100. The AChR-LP had a specificity of 1.61 +/- 1.12 nmol of alpha-bungarotoxin binding sites per mg of protein. The isoelectric point, sedimentation coefficient and amino acid composition of the purified AChR-LP were very similar to those of muscle and electric organ AChRs. Upon SDS-polyacrylamide gel electrophoresis purified thymus AChR-LP preparations contained up to 6 polypeptide bands of molecular weights of 40,000, 43,000, 51,000, 56,000, 58,000, and 66,000, respectively. The peptides of 40,000, 51,000, 56,000, and 66,000 dalton cross-reacted with the four subunits of Torpedo californica and fetal calf muscle AChR.