[Isolation and primary characterization of two forms of inorganic pyrophosphatase from ox heart muscle mitochondria].

A method allowing to obtain two highly purified forms (membrane-bound and soluble ones) of inorganic pyrophosphatase from bovine heart mitochondria is described. Both forms have the isoelectric point of 5.8, pH optimum with Mg2+ at 7--9, are maximally stable at pH 5.8 and absolutely specific to PPi and require Mg2+ or Co2+ for their activity. The soluble pyrophosphatase is also activated by Zn2+. Besides, the two forms differ in their electrophoretic mobilities, affinity for DEAE cellulose and stability in acidic (pH less than 5.8) and alkaline media.