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  • Title: [Purification and characteristics of Saccharomyces cerevisiae cytosol polyphosphatase].
    Author: Andreeva NA, Kulakovskaia TV, Kulaev IS.
    Journal: Biokhimiia; 1996 Sep; 61(9):1714-24. PubMed ID: 8998291.
    Abstract:
    The polyphosphatase with specific activity of 283 units/mg was purified 3450-fold to homogeneity with 3.8% yield from cytosol of Saccharomyces cerevisiae yeast. Polyphosphatase is monomeric 40 kD protein. The enzyme hydrolyzes polyphosphates of various chain length including tripolyphosphate but ATP, pyrophosphate, and p-nitrophenyl phosphate are not the substrates. Enzyme activity is maximal at 50 degrees C and pH 6.5-8.5. Several cations of bivalent metals stimulated the enzyme activity 8-66-fold (Co2+ > Mn2+ > Mg2+ > Zn2+ > Fe2+). The enzyme is inactive in the presence of Ca2+ or Cu2+. Heparin, antibodies against cell-envelope polyphosphatase, and Cu2+ or Zn2+ in the presence of Mg2+ are potent inhibitors of cytosolic polyphosphatase. Cytosolic polyphosphatase is similar to purified cell-envelope polyphosphatase but differs in some properties from nuclear, vacuolar, and mitochondrial polyphosphatase of the very same yeast.
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