The acetylcholine receptor as part of a protein complex in receptor-enriched membrane fragments from Torpedo californica electric tissue.
The acetylcholine receptor from Torpedo californica electric tissue consisting of polypeptide chains of molecular weight 42000 (+/- 2000) is part of a protein complex. Cross-linking experiments with bifunctional reagents have shown that this complex has possibly a pentameric structure with a molecular weight of 270000 (+/- 30000). Besides the receptor subunit (alpha-chain), at least three further classes of polypeptide chains are part of the complex: beta (Mr 48000), gamma (Mr 62000) and delta (Mr 68000). This can be shown by cross-linking the proteins extracted from receptor-enriched membrane fractions with a cleavable reagent: From the 270000 molecular weight particle the four predominant polypeptide chains of the membrane, alpha, beta, gamma, and delta, can be obtained. The gamma-polypeptide chains appear to form a dimer connected by an inter-chain disulphide bridge.
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004220:Disulfides / Q000032:analysis; D004557:Electric Organ / Q000378:metabolism*; D005399:Fishes; D046911:Macromolecular Substances; D008970:Molecular Weight; D011950:Receptors, Cholinergic / Q000302:isolation & purification* / Q000378:metabolism
D004220:Disulfides; D046911:Macromolecular Substances; D011950:Receptors, Cholinergic; D000109:Acetylcholine