Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE)

Autor: W N, Kuo, U, Ganesan, D L, Walbey, D L, Davis, K, Allen, L K, McCall
Rok vydání: 1993
Předmět:
Zdroj: Applied and theoretical electrophoresis : the official journal of the International Electrophoresis Society. 3(6)
ISSN: 0954-6642
Popis: 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.
Databáze: OpenAIRE