title: Purification and characterization of alkaline phosphatase from cultured rat ascites hepatoma cells.
abstract: 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.
mesh_terms: D000469:Alkaline Phosphatase / Q000302:isolation & purification* / Q000378:metabolism; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D002478:Cells, Cultured; D004355:Drug Stability; D006023:Glycoproteins / Q000302:isolation & purification; D007700:Kinetics; D008113:Liver Neoplasms / Q000201:enzymology*; D046911:Macromolecular Substances; D008722:Methods; D008970:Molecular Weight; D009374:Neoplasms, Experimental / Q000201:enzymology
chemical_list: D006023:Glycoproteins; D046911:Macromolecular Substances; D000469:Alkaline Phosphatase