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.
D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002247:Carbon Isotopes; D002415:Cats; D002540:Cerebral Cortex / Q000378:metabolism*; D002845:Chromatography; D002855:Chromatography, Thin Layer; D003902:Detergents / Q000494:pharmacology; D008074:Lipoproteins / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism*; D009186:Myelin Sheath / Q000378:metabolism*; D009411:Nerve Endings / Q000378:metabolism*; D011485:Protein Binding; D011955:Receptors, Drug; D014403:Tubocurarine / Q000378:metabolism*
D002247:Carbon Isotopes; D003902:Detergents; D008074:Lipoproteins; D011955:Receptors, Drug; D000110:Acetylcholinesterase; D014403:Tubocurarine