title: Purification and heterogeneity of inorganic pyrophosphatase of pig scapula cartilage.
abstract: Inorganic pyrophosphatase (pyrophosphate phosphohydrolase; EC 3.6.1.1) was purified from pig scapula cartilage by fractionation with N-cetylpyridinium chloride and (NH4)2SO4, followed by ion-exchange and gel-filtration chromatography. Enzyme preparations of high purity were obtained, with specific activities (100-400 units/mg) higher than those previously described for mammalian pyrophosphatases. The enzyme activity could be separated into several subfractions on ion-exchange columns.
mesh_terms: D000469:Alkaline Phosphatase / Q000032:analysis; D000645:Ammonium Sulfate; D000818:Animals; D002356:Cartilage / Q000201:enzymology*; D002594:Cetylpyridinium; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D011506:Proteins / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis; D011755:Pyrophosphatases / Q000032:analysis / Q000302:isolation & purification*; D012540:Scapula / Q000201:enzymology; D013552:Swine
chemical_list: D011506:Proteins; D011509:Proteoglycans; D002594:Cetylpyridinium; D000469:Alkaline Phosphatase; D011755:Pyrophosphatases; D000645:Ammonium Sulfate