Neurochemical Research

, Volume 8, Issue 7, pp 865–871 | Cite as

The in vitro phosphorylation of actin from rat cerebral cortex

  • Peter R. Dunkley
  • Phillip J. Robinson
Original Articles


Actin was phosphorylated by a cyclic AMP-stimulated protein kinase in a lysed synaptosomal fraction incubated with [γ-32P]ATP, while calcium had no effect on endogenous labeling of the protein. Incubation of an intact synaptosomal fraction with32P-inorganic phosphate did not lead to any detectable phosphorylation of actin in the presence or absence of dibutryl-cyclic AMP, or chemical depolarization. It is suggested that actin is not phosphorylated in the physiologically relevant intact synaptosomes but gains access to protein kinases on lysis.


Calcium Phosphate Protein Kinase Cerebral Cortex Gain Access 
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Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

  • Peter R. Dunkley
    • 1
  • Phillip J. Robinson
    • 1
  1. 1.The Neuroscience Group Faculty of MedicineUniversity of Newcastle

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