|
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 |
Family |
2.6.1.52.a |
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 |
2020/02/20 10:46 |
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