Antibodies to a synthetic peptide corresponding to residues 346-359 of the Torpedo acetylcholine receptor (AChR) γ subunit, were employed to compare the adult and embryonic receptor. This peptide contains a consensus phosphorylation site for cAMP-dependent protein kinase (PKA). The anti-peptide antibodies discriminated between adult and embryonic AChRs, and reacted preferentially with the adult γ form. These observed immunological differences did not seem to stem from different phosphorylation states. Our results suggest that the embryonic Torpedo AChR may have a γ-like subunit that differs from the known adult form of this subunit, at least in the specific region that contains the phosphorylation site for PKA.
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Acknowledgements: This work was supported by grants from the Association FrancaiseC ontre Its Myopathies( AFM), the Los Angeles Chapter of the Myasthenia Gravis Foundation, the Muscular Dystrophy Association of America, the United Stt!cs-Israel Binational Science Foundation and the Schilling Foundation.