Cholinergic binding capacity of proteolipids from isolated nerve-ending membranes.

The capacity for binding dimethyl d-tubocurarine-C(14) was studied in isolated nerve-ending membranes from cerebral cortex and myelin. After treatment of the membrane with organic solvents most of the radioactivity was recovered in the extract. Preliminary evidence indicates that dimethyl d-tubocurarine-C(14) is not bound to lipids or glycolipids. While the proteolipids of myelin have a low binding capacity, the results obtained with the nerve-ending membranes rich in acetylcholinesterase suggest that the cholinergic receptor may be a special type of proteolipid.