ITEM METADATA RECORD
Title: The control of phosphorylase kinase phosphatase activity by polycations and the deinhibitor protein
Authors: Goris, Jozef ×
Walsh, D A
Merlevede, Wilfried #
Issue Date: Jan-1985
Series Title: Biochemical and Biophysical Research Communications vol:125 issue:1 pages:293-8
Abstract: The dephosphorylation of phosphorylase beta kinase by the activated ATP, Mg-dependent protein phosphatase, which is highly specific for the beta-subunit, is stimulated by the deinhibitor protein which neutralizes the effect of inhibitor-1 and the modulator protein on the phosphatase. The specific dephosphorylation of the alpha-subunit of phosphorylase beta kinase by a "latent" protein phosphatase isolated from vascular smooth muscle is stimulated by histone H1 but not affected by the deinhibitor protein. These observations show that there is no strict correlation between the insensitivity of a protein phosphatase to inhibitor-1 or modulator protein and the dephosphorylation of the alpha-subunit of phosphorylase beta kinase.
URI: 
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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