Muscarinic Receptor Purification and Properties

  • Michael Schimerlik
Part of the The Receptors book series (REC)


The solubilization and purification of mAChR has proven to be a rather difficult problem because of a low density of receptor sites, poor yields of solubilized protein upon detergent extraction, and receptor instability in many commonly used, inexpensive detergents. Initial studies indicated that the detergent digitonin was capable of solubilizing muscarinic binding sites from the brain (Beld and Ariens, 1974; Hurko, 1978; Aronstam et al., 1978; Gorissen et al., 1978). Since most commercial preparations of digitonin are heterogeneous, containing 70–80% digitonin, 10–20% gitonin and tigonin, plus 5–15% minor saponins, the composition of the solubilizing agent is poorly defined. The variability in efficiency of receptor solubilization and the solubility of the detergent itself in aqueous solution are most probably related to differing digitonin compositions that, in turn, depend on the lot number and supplier. In studies on receptor solubilization from the rat brain (Repke and Matthies, 1980), optimal results were obtained using a defined mixture of 3 digitonin/2 gitonin (w/w).


Muscarinic Receptor Muscarinic Acetylcholine Receptor Muscarinic Agonist Guanine Nucleotide Binding Protein Muscarinic Receptor Subtype 
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© The Humana Press Inc. 1989

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  • Michael Schimerlik

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