Lund K, Merrill D K, Guynn R W
Arch Biochem Biophys. 1987 Apr;254(1):319-28. doi: 10.1016/0003-9861(87)90108-1.
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.
通过非变性和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、分析超速离心及免疫化学分析判断，L-磷酸丝氨酸转氨酶从牛肝脏中纯化至表观均一。所述纯化程序包括通过微摩尔浓度的底物磷酸羟基丙酮酸从Cibacron蓝琼脂糖上特异性洗脱该酶。纯化后的酶在38℃下的比活性约为每分钟每毫克蛋白质形成13微摩尔磷酸羟基丙酮酸。天然分子量和亚基分子量的测定表明，来自牛肝脏的磷酸丝氨酸转氨酶是由两个分子量均为43,000的亚基组成的二聚体。
