The Acetylcholine Receptor as Part of a Protein Complex in Receptor-Enriched Membrane Fragments from Torpedo californica Electric Tissue
European Journal of BiochemistryPublished 1 February 1978Open access
Ferdinand Hucho, Giampiero Bandini, Benjamín A. Suárez‐Isla
Citations79
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TL;DR
The acetylcholine receptor from Torpedo californica electric tissue consisting of polypeptide chains of molecular weight 42000 (+/- 2000) is part of a protein complex that has possibly a pentameric structure with a molecular weight of 270000 (+/- 30000).
Abstract
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.
Keywords
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