Biochemical properties of acteylcholine receptor subunits from Torpedo californica

Abstract

Four polypeptide chains composing acetylcholine receptors from the electric organ of Torpedo californica were purified by preparative electrophoresis in sodium dodecyl sulfate. Their apparent mole ratio alpha/beta/gamma/delta is 2:1:1:1. These chains are not readily distinguished by amino acid or carbohydrate composition but are distinguished by apparent molecular weight and polypeptide maps. By peptide maps, no extensive homology is evident between these chains or between any of these chains and higher molecular weight chains found in receptor-enriched membrane fragments.