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Further characterization of mitochondrial protein phosphatase

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
166
Issue
1
Identifiers
DOI: 10.1016/0003-9861(75)90393-8
Keywords
  • Enzyme Mechanisms And Metabolism
Disciplines
  • Biology

Abstract

Abstract Mitochondrial protein phosphatase from rat liver exhibits rather wide substrate specificity, since it readily dephosphorylates, besides phosvitin, casein, and cytosol phosphoproteins, also ATP, ADP, inorganic pyrophosphate, p-nitrophenylphosphate. Aliphatic phosphate esters (β-glycerophosphate, glucose-6- P, serine-phosphate) are not dephosphorylated to any detectable extent. Evidence for the participation of a single enzyme in the dephosphorylation of phosvitin and ATP is provided. However, the different affinity toward the two substrates and other evidence suggest that the enzyme has in vivo the biological role of dephosphorylating, at least preferentially, the phosphoproteins.

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