The Isolation of Functional Acetylcholine Receptor

Abstract

In current studies on the purification of acetylcholine receptor, efforts have been directed towards purification of that component of the receptor which bears the recognition site or sites. Consequently, we do not use the term ‘functional’ in the sense that we propose to describe purification of receptor macromolecules which contain the whole apparatus of recognition and (after insertion into an appropriate membrane) transduction. Instead we mean ‘functional’ to imply only that the purified macromolecule can recognize and bind its own transmitter. In particular, we are concerned to contrast the use of the technique which we shall call the reversible ligand technique, and which generally employs acetylcholine as the ligand, with techniques in which ‘irreversibly’ bound α-bungarotoxin (BuTX) is used as a label.