Phosphorylation of brain muscarinic receptor: evidence of receptor regulation.

@article{Ho1987PhosphorylationOB,
  title={Phosphorylation of brain muscarinic receptor: evidence of receptor regulation.},
  author={A. Ho and Q. Ling and R. Duffield and P. H. Lam and J. Wang},
  journal={Biochemical and biophysical research communications},
  year={1987},
  volume={142 3},
  pages={
          911-8
        }
}
  • A. Ho, Q. Ling, +2 authors J. Wang
  • Published 1987
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
Muscarinic receptor, from porcine synaptic membrane, was purified by affinity chromatography. Molecular weight analysis by SDS-gel electrophoresis revealed one major peptide with an apparent Mr of 68 +/- 2 Kda. The purified receptor was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase resulting in a concomitant loss in specific binding, and this loss was reversed by calcineurin. 
Phosphorylation by Protein Kinase C of the Muscarinic Acetylcholine Receptor
Diversity of structure, signaling and regulation within the family of muscarinic cholinergic receptors
  • M. Hosey
  • Biology, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1992
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