Yokota Y
J Biochem. 1978 May;83(5):1293-8. doi: 10.1093/oxfordjournals.jbchem.a132036.
Alkaline phosphatase of cultured rat ascites hepatoma cells has been purified by butanol extraction, DEAE-cellulose column chromatography, gel filtration through Sephadex G-200, concanavalin A-Sepharose affinity chromatography, and polyacrylamide gel electrophoresis. Affinity chromatography confirmed the glycoprotein nature of alkaline phosphatase from cultured rat ascites hepatoma cells. Electrophoresis on polyacrylamide gels of various concentrations indicated a molecular weight of 290,000. The molecular weight of the subunit was estimated to be 72,000 by SDS-polyacrylamide gel electrophoresis. These findings suggest that alkaline phosphatase of cultured rat ascites hepatoma cells is a tetramer with a subunit molecular weight of 72,000.
通过丁醇萃取、DEAE - 纤维素柱色谱、Sephadex G - 200凝胶过滤、伴刀豆球蛋白A - 琼脂糖亲和色谱以及聚丙烯酰胺凝胶电泳，对培养的大鼠腹水肝癌细胞碱性磷酸酶进行了纯化。亲和色谱证实了培养的大鼠腹水肝癌细胞碱性磷酸酶的糖蛋白性质。在不同浓度聚丙烯酰胺凝胶上进行电泳表明其分子量为290,000。通过SDS - 聚丙烯酰胺凝胶电泳估计亚基的分子量为72,000。这些发现表明，培养的大鼠腹水肝癌细胞碱性磷酸酶是一种亚基分子量为72,000的四聚体。
