Neurochemical Research

, Volume 6, Issue 2, pp 203–211 | Cite as

Increased phosphorylation in vitro of a cytosolic polypeptide resolved from denervated skeletal muscle

  • Stephen P. Squinto
  • Jerry A. McLane
  • Irene R. Held
Original Articles

Abstract

The in vitro phosphorylation of a 40,400-dalton, cytosolic polypeptide from the soleus muscle of the rat is increased twofold within 24 hr after cutting the motor nerve fibers to this muscle. This involves an ATP:phosphotransferase reaction which we have reported to be inhibited by a specific cyclic AMP-dependent protein kinase inhibitor. The phosphorylated polypeptide does not electrophoretically comigrate on SDS-polyacrylamide gels with the 38,000-dalton catalytic subunit of cyclic AMP-dependent protein kinase which is known to undergo a site-specific autophosphorylation in skeletal muscle.

Keywords

Skeletal Muscle Protein Kinase Polypeptide Nerve Fiber Kinase Inhibitor 

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Copyright information

© Plenum Publishing Corporation 1981

Authors and Affiliations

  • Stephen P. Squinto
    • 1
    • 2
  • Jerry A. McLane
    • 1
    • 2
  • Irene R. Held
    • 1
    • 2
  1. 1.Neuroscience Research ProgramVeterans Adminitration HospitalHines
  2. 2.Departments of Biochemistry and PharmacologyLoyola University Stritch School of MedicineMaywood

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