Purification and Characterization of Hepatic Inorganic Pyrophosphatase Hydrolyzing Imidodiphosphate

A 56-kDa inorganic pyrophosphatase consisting of 33-kDa subunits was purified from bovine liver almost to homogeneity. This hydrolase required divalent cations such as MgCl2, CoCl2, and MnCl2to hydrolyze PPiand was insensitive to 2 mmsodium fluoride. The purified hydrolase released 2.1 μmol Pifrom P...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1997-05, Vol.341 (1), p.153-159
Hauptverfasser:	Hiraishi, Hiroyuki, Ohmagari, Takao, Otsuka, Yasufumi, Yokoi, Fumiaki, Kumon, Akira
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals bovine liver Cations, Divalent - pharmacology Cattle characterization Diphosphonates - metabolism Electrophoresis, Polyacrylamide Gel Hydrogen-Ion Concentration Hydrolysis hydrolysis of imidodiphosphate Inorganic Pyrophosphatase Liver - enzymology Metals - pharmacology Molecular Weight Protein Denaturation purification Pyrophosphatases - antagonists & inhibitors Pyrophosphatases - chemistry Pyrophosphatases - isolation & purification Pyrophosphatases - metabolism Sodium Dodecyl Sulfate Substrate Specificity Sulfhydryl Reagents - pharmacology Temperature Ultracentrifugation
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