Purification and Properties of Alkaline Phosphatase with Protein Phosphatase Activity from Saccharomyces cerevisiae

@inproceedings{Galabova2000PurificationAP,
  title={Purification and Properties of Alkaline Phosphatase with Protein Phosphatase Activity from Saccharomyces cerevisiae},
  author={Danka Galabova and Borijana Tuleva and Evgenia Vasileva-Tonkova and Nelly E Christova},
  year={2000}
}
An alkaline phosphatase (A LPase) from Saccharomyces cerevisiae strain 257 was purified 345-fold with specific activity of 54 533 nmol x min“ 1 x mg protein-1 . It was shown to be a dimeric protein (apparent mol. wt. approx. 130 kDa) with optimum activity at pH 8.6 8.8 and good stability at 50 °C. The A LPase was a non-specific enzyme hydrolyzing a wide vari­ ety of monophosphate esters. The enzyme showed protein phosphatase activity and this activ­ ity was not Mg2+ dependent in contrast to… CONTINUE READING
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