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  • Title: Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE).
    Author: Kuo WN, Ganesan U, Walbey DL, Davis DL, Allen K, McCall LK.
    Journal: Appl Theor Electrophor; 1993; 3(6):317-20. PubMed ID: 8199224.
    Abstract:
    The proteolysis of the 32P-labeled holoenzyme of cyclic AMP-dependent protein kinase (A-PKII:DEAE, peak II fraction) was analysed by SDS-polyacrylamide gel electrophoresis and autoradiography. The contaminants of the A-PKII and calpain II apparently did not interfere with the accuracy of this highly sensitive analysis. Phosphorylation of calpain II by the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK) greatly enhanced the proteolysis of A-PKII, whereas phosphorylation by protein kinase C (PK-C) or cyclic GMP-dependent protein kinase (G-PK) slightly altered the proteolysis.
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