Title: Isolation of an active form of the ATP + Mg2+-dependent protein phosphatase stimulated by the deinhibitor protein and by p-nitrophenyl phosphate
Authors: Goris, Jozef ×
Merlevede, Wilfried #
Issue Date: Nov-1988
Series Title: The Biochemical journal. vol:254 issue:2 pages:501-7
Abstract: A 75 kDa + 37 kDa-subunit high-Mr form of the ATP + Mg2+-dependent phosphatase, containing no modulator or inhibitor-1 and specific towards the beta-subunit of phosphorylase kinase, was isolated from dog liver. The phosphorylase phosphatase activity is stimulated by the deinhibitor protein, by p-nitrophenyl phosphate or by trypsin treatment. The sensitivity to modulator or inhibitor-1 can be increased dramatically by partial proteolysis. The enzyme inactivation by modulator after trypsin treatment can be reversed by protein kinase FA. The effects of p-nitrophenyl phosphate and the deinhibitor protein are synergistic, and p-nitrophenyl phosphate does not influence the sensitivity of the phosphatase to the heat-stable inhibitor proteins. These observations confirm that p-nitrophenyl phosphate stimulation is a suitable criterion for the identification of the active enzyme forms of the ATP + Mg2+-dependent phosphatase.
ISSN: 0264-6021
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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