Purification and properties of an acid phosphoprotein phosphatase from Tetrahymena pyriformis.
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.
Lougovoi
C P
CP
Laboratory of Biochemistry, Faculty of Chemistry, Aristotelian University of Thessaloniki, Greece.
Paterakis
A
A
Kyriakidis
D A
DA
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002845:Chromatography / Q000379:methods; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D013379:Substrate Specificity; D013769:Tetrahymena pyriformis / Q000201:enzymology*
D011732:Pyridoxal Phosphate; D000255:Adenosine Triphosphate; D010749:Phosphoprotein Phosphatases