Abstract
Nicotinic acetylcholine receptor (AChR) was purified from denervated and normal rabbit muscle using two affinity chromatography steps. Examination of the purified AChRs, radiolabeled with Na 125I, with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed identical patterns for both AChRs, consisting of 4 polypeptide bands with apparent M rs of 42, 44, 52 and 68 Kdaltons and a broad band in the 58 kdalton region. The sedimentation coefficient for both AChRs was 9 S, a value corresponding to the monomeric form of Torpedo AChR. The 42 Kdaltons subunit of denervated AChR was labeled by the affinity alkylating reagent [ 3H]4-(N-maleimido)phenyltrimethylammonium. Antiactin serum binds to the 44 kdalton polypeptide. Sera which had high titer against human AChR and veal AChR precipitated denervated AChR indicating a high degree of homology within mammalian AChRs.
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