Activities | Families | Sequences | Fold types | References | Help
B6db references: 87212005

type Journal Article
authors Lund, K.; Merrill, D. K.; Guynn, R. W.
title Purification and properties of phosphoserine aminotransferase from bovine liver
journal Arch Biochem Biophys
Activity 2.6.1.52
ui 87212005
year (1987)
volume 254
number 1
pages 319-28.
 
keywords Animal
abstract 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.
last changed 2002/11/12 16:17

B6db references