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.[1]References
- Purification and properties of phosphoserine aminotransferase from bovine liver. Lund, K., Merrill, D.K., Guynn, R.W. Arch. Biochem. Biophys. (1987) [Pubmed]
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