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Characterization of protein phosphorylation in acetylcholine receptor-enriched membrane preparations from torpedo fuscomaculata

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Summary

When the acetylcholine receptor (AChR*) from Torpedo is phosphorylated, ATP is found to bind non-covalently to the preparation. After correction is made for this binding of ATP, the phosphorylation reaction has a Km of 0,16 mM, a pH optimum of 8,6 and reaches maximal activity within 3 min. The intrinsic kinase activity is very specific for the AChR and does not phosphorylate either histones or phosvitin. The only amino acid to be phosphorylated is serine and cyclic GMP causes stimulation of the reaction.

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Abbreviations

AChR:

acetylcholine receptor

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Authors and Affiliations

  1. Neurochemistry Research Group, Department of Chemical Pathology, University of Stellenbosch, P. O. Box 63, 7505, Tygerberg, South Africa

    M. E. Carstens, M. Weller, A. C. Neethling & J. J. F. Taljaard

Authors
  1. M. E. Carstens
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  2. M. Weller
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  3. A. C. Neethling
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  4. J. J. F. Taljaard
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Carstens, M.E., Weller, M., Neethling, A.C. et al. Characterization of protein phosphorylation in acetylcholine receptor-enriched membrane preparations from torpedo fuscomaculata. Mol Cell Biochem 42, 161–166 (1982). https://doi.org/10.1007/BF00238510

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  • DOI: https://doi.org/10.1007/BF00238510

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