Purification and properties of phosphoserine aminotransferase from bovine liver.
L-Phosphoserine aminotransferase was purified from bovine liver to apparent homogeneity as judged by nondenaturing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, analytical ultracentrifugation, and immunochemical analysis. The purification procedure described involves the specific elution of the enzyme from Cibacron blue-agarose by micromolar concentrations of its substrate, phosphohydroxypyruvate. The purified enzyme had a specific activity of approximately 13 mumol of phosphohydroxypyruvate formed min-1 mg-1 of protein at 38 degrees C. Determinations of the native molecular weight and the subunit molecular weight indicated that the phosphoserine aminotransferase from bovine liver was a dimer composed of two subunits with identical molecular weights of 43,000.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D000637:Transaminases / Q000276:immunology / Q000302:isolation & purification*
D000637:Transaminases; C022393:phosphoserine aminotransferase