Related Experiment Videos
Purification and properties of an acid phosphoprotein phosphatase from Tetrahymena pyriformis
C P Lougovoi1, A Paterakis, D A Kyriakidis
1Laboratory of Biochemistry, Faculty of Chemistry, Aristotelian University of Thessaloniki, Greece.
Biochemistry International
|November 1, 1988
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.