Studies on a cAMP-Dependent Protein Kinase Obtained from Nicotinic Receptor-Bearing Microsacs

  • H. Eriksson
  • R. Salmonsson
  • G. Liljeqvist
  • E. Heilbronn
Part of the Advances in Behavioral Biology book series (ABBI, volume 30)


The nicotinic acetylcholine receptor (nAChR) of Torpedo californica is composed of four different subunits with apparent relative molecular Mr of 40,000 (α), 50,000 (β), 60,000 (γ) and 66,000 (δ) with 2:1:1:1 stoichiometry in the monomer (4, 14). In the receptor-containing membranes from electric organs of the same fish, a protein kinase is present which is able to phosphorylate the γ- and δ-subunits (3, 6, 7, 15, 17). This phosphorylation has been regarded as cyclic nucleotide independent (6, 15, 17) until recently, when Huganir and Greengard (10) found that cAMP stimulates the endogenous phosphorylation of nAChR from the electric organ of Torpedo californica.


Protein Kinase Activity Electric Organ Protease Inhibitor Mixture Swedish Natural Science Research Council Endogenous Phosphorylation 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • H. Eriksson
    • 1
  • R. Salmonsson
    • 1
  • G. Liljeqvist
    • 1
  • E. Heilbronn
    • 1
  1. 1.Unit of Neurochemistry and NeurotoxicologyUniversity of StockholmSundbybergSweden

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