Abstract
Summary Hydrophobic protein fractions, having nicotinic or muscarinic binding properties were separated respectively from skeletal muscle and smooth intestinal muscle using the lipophilic gel Sephadex LH2O. Further purification of the specific fractions was carried out by a cholinergic affinity column, using elution with organic solvents, followed by a pulse of 10−3M acetylcholine . The results obtained confirm the validity of the Sephadex LH20 technique for the isolation and binding of cholinergic proteins proposed by De Robertis et al (4) and discard the criticisms raised by Levinson and Keynes (7).
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