title: Some properties of inorganic pyrophosphatase from Bacillus subtilis.
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.
authors.affiliation: Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
authors.forename: M
authors.initials: M
authors.lastname: Imai
authors.forename: S
authors.initials: S
authors.lastname: Araki
authors.forename: K
authors.initials: K
authors.lastname: Kishida
authors.forename: Y
authors.initials: Y
authors.lastname: Terasawa
authors.forename: A
authors.initials: A
authors.lastname: Hachimori
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D004734:Energy Metabolism; D011755:Pyrophosphatases / Q000032:analysis* / Q000378:metabolism
chemical_list: D011755:Pyrophosphatases