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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 14 (1980), S. 13-19 
    ISSN: 0091-7419
    Keywords: properties of acetylcholine receptor ; reconstitution of acetylcholine receptor ; subunit composition of acetylcholine receptor ; proteolysis of acetylcholine receptor ; Ca2+ activated protease ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Purified acetylcholine receptor reconstituted into liposomes catalyzes carbamylcholine-dependent ion flux [10]. An endogenous protease activated by Ca2+ gives rise to an acrylamide gel pattern of the receptor with the 40,000-dalton subunit apparently as the major component. Exogenous proteases nick the proteins so extensively that the acrylamide gel pattern reveals polypeptides of 20,000 daltons or less. In either case the receptor sediments at 9S, indicating that the polypeptide chains associated. Moreover, the nicked receptors bind α-bungarotoxin and catalyze carbamylcholine-dependent ion flux after reconstitution.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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