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  • Title: Some properties of inorganic pyrophosphatase from Bacillus subtilis.
    Author: Shimizu T, Imai M, Araki S, Kishida K, Terasawa Y, Hachimori A.
    Journal: Int J Biochem Cell Biol; 1997 Feb; 29(2):303-10. PubMed ID: 9147131.
    Abstract:
    Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1; PPase) from Bacillus subtilis was purified to a homogeneous state electrophoretically when analysed by SDS-PAGE. The enzyme consists of six identical subunits; the molecular weight of the native enzyme estimated by gel filtration was approx. 120,000, and denaturing polyacrylamide gel electrophoresis gave a single band corresponding to 24,000. The enzyme absolutely required a divalent cation for its activity. Mg2+ was most effective, showing two steps of concentration-dependent activation. Mg2+ could be partially replaced by Mn2+ and Co2+. The enzyme was thermostable in the presence of Mg2+, and no loss of activity was observed on the incubation at 55 degrees C for an hour.
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