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  • Title: Photoaffinity labeling of the solubilized, partially purified muscarinic acetylcholine receptor from porcine atria by p-azidoatropine methyl iodide.
    Author: Cremo C, Schimerlik MI.
    Journal: Biochemistry; 1984 Jul 17; 23(15):3494-501. PubMed ID: 6547852.
    Abstract:
    The synthesis of a tritiated photoaffinity analogue of the muscarinic antagonist atropine, [3H]-p-azidoatropine methyl iodide is described. The compound appeared to bind to a single class of sites in membrane-bound, solubilized, and partially purified preparations of muscarinic receptor from porcine atria with a dissociation constant (determined by competition vs. [3H]-L-quinuclidinyl benzilate) of about 1.0 X 10(-7) M. This value was in agreement with the apparent dissociation constant (8.5 X 10(-8)M) determined by measuring the concentration dependence of covalent incorporation into a partially purified receptor preparation. Competition experiments indicated that the specific covalent labeling could be blocked by the muscarinic agonist carbamylcholine and the antagonists L-quinuclidinyl benzilate and atropine. An apparent molecular weight of 75 000 +/- 5000 was found for specifically labeled peptide(s) in a solubilized, partially purified receptor preparation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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