Purification and properties of an acid phosphoprotein phosphatase from Tetrahymena pyriformis |
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| Authors: | C P Lougovoi A Paterakis D A Kyriakidis |
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| Institution: | Laboratory of Biochemistry, Faculty of Chemistry, Aristotelian University of Thessaloniki, Greece. |
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| Abstract: | A cytosolic acid phosphoprotein phosphatase was purified by ion exchange (DEAE-Biogel A, DE-52) and hydrophobic (Phenyl-Sepharose) chromatography. The purified phosphoprotein phosphatase was homogeneous as judged by polyacrylamide gel electrophoresis under native or denature conditions. The enzyme has a Mr of 90.000. The Km value and the optimum pH determined with p-nitrophenyl phosphate was 0.3 mM and 4.0, respectively. The enzyme is inhibited by NaF, ATP, 5'-pyridoxal phosphate and slightly activated by divalent cations. |
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