Abstract
A cholinergic proteolipid fraction (i.e. a hydrophobic lipoprotein) was separated from the n. caudatus of the cow, using affinity chromatography with the lipophilic gel Sephadex LH-20 and p-phenyltrimethylamonium as the active group. High affinity binding studies showed that only the specific fraction, desorbed after an acetylcholine (or acid) pulse, and corresponding to 0,72% of the proteolipids, is the one that binds the cholinergic ligands. The binding of ( 3H)atropine and ( 14C)d-tubocurarine demonstrated that there are 814 picomoles/g fresh tissue of muscarinic sites and only 76 picomoles/g of nicotinic sites. The specific radioactivity for ( 3H)atropine is 10,000 nmoles/g protein, suggesting a high degree of purification of the specific cholinergic proteolipid.
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