Further characterization of mitochondrial protein phosphatase. |
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Authors: | G Clari A Donella L A Pinna V Moret |
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Affiliation: | Istituto di Chimica Biologica dell''Università di Padova and “Centro per lo Studio della Fisiologia dei Mitocondri” del C.N.R., Padova, Italy |
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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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