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- W2017506494 abstract "Four subunits of the acetylcholine receptor molecule, obtained from the electric organ of Torpedo ocellata, have been isolated using polyacrylamide gel electrophoresis, and assayed by titration with a fluorescent lanthanide, terbium, and by affinity-labeling with p-(N-maleimido)benzyl [trimethyl-3H] ammonium iodide. The site with which the activator-analogue affinity label reacts, as well as the terbium-binding sites, are mainly associated with the smallest of the subunits of an apparent molecular weight of 40,000. Calcium competes with terbium for these binding sites. The affinity for terbium is the same in the intact molecule as in the subunit (KTb ⋍ 19 ± 1 μM), but the affinity for calcium decreases by a factor of 4 (KCa ⋍ 4 mM) in the subunit. Hydrolysis of the receptor, catalyzed by trypsin and chymotrypsin, to peptides with an apparent molecular weight of 8000 or less, does not affect the terbium-binding sites. These experiments indicate that the binding sites for neural activators and for calcium are associated with the same subunit, and that the terbium- and calcium-binding sites reflect structural properties of the polypeptide chain rather than the three-dimensional structure of the protein." @default.
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- W2017506494 title "Identification of a calcium-binding subunit of the acetylcholine receptor" @default.
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- W2017506494 doi "https://doi.org/10.1016/0006-291x(76)90694-x" @default.
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