The Role of the α and β Subunits in the Regulation of Phosphorylase Kinase Activity

  • Philip Cohen
  • John F. Antoniw
  • Michael Davison
  • Carol Taylor
Conference paper

Abstract

The reversible activation of phosphorylase kinase catalysed by cyclic AMP1 dependent protein kinase and phosphorylase kinase phosphatase is shown to be associated with the reversible phosphorylation of a unique site on the β-subunit of the enzyme, and the isolation and analysis of a tryptic phosphopeptide containing the phosphorylated site is described. The phosphorylation of a second site, on the α-subunit, does not affect activity directly, but is shown to control the rate of dephosphorylation of the β-subunit by phosphorylase kinase phosphatase. The role of the three subunits of phosphorylase kinase, α, β and γ is discussed in terms of electron micrographs of the molecule.

Keywords

Adenosine Lysine Arginine Pyruvate Trypsin 

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1974

Authors and Affiliations

  • Philip Cohen
    • 1
  • John F. Antoniw
    • 1
  • Michael Davison
    • 1
  • Carol Taylor
    • 1
  1. 1.Department of BiochemistryMedical Sciences Institute, The UniversityDundeeScotland

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