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  • Title: Inorganic pyrophosphatase--II. Purification and studies of some properties of the enzyme isolated from thermophylic bacterium Thermus flavus 70 K.
    Author: Kasho VN, Avaeva SM.
    Journal: Int J Biochem; 1984; 16(3):315-21. PubMed ID: 6141964.
    Abstract:
    Inorganic pyrophosphatase was isolated from T. flavus in a homogeneous form with a specific activity of 400 U/mg. The enzyme has an isoelectric point 5.0 and consists of 4 subunits each of 24,000 mol. wt. Pyrophosphatase possesses high thermal stability. The enzyme can hydrolyze PPi, ATP and p-nitrophenylphosphate. Kinetic constants of the enzyme's interaction with the metal-activator and metal-substrate complex have been estimated.
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