The glycoprotein nature of solubilized muscarinic acetylcholine receptors from bovine cerebral cortex

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Summary

Muscarinic acetylcholine receptors were solubilized from bovine cerebral cortex with 3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate. The so-obtained receptors could be precipitated by Wheat Germ (73%), Concanavalin A (55 %), Lens Culinaris (36 %) and Ricinus Communis (26 %), but not by Peanut, Dolichus Biflorus and Ulex Europaeus. On Wheat Germ- and Concanavalin A-affinity chromatography, the solubilized muscarinic receptors were retained on both columns and subsequently eluted with N-acetylglucosamine and α-methyl-D-mannoside, respectively. A high concentration (100 μg/ml) of Wheat Germ or Concanavalin A did not interfere with Z-[3H]quinuclidinyl benzilate binding, thereby suggesting that the lectin binding sites are not directly involved in the receptor binding function. These solubilized muscarinic receptors are postulated to contain carbohydrate residues, N-acetylglucosamine, mannose and galactose, as glycoprotein.

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