Phosphorylase Phosphatase Activity in Saccharomyces cerevisiae 257

Abstract Phosphorylase Phosphatase, Protein Phosphatase, Saccharomyces cerevisiae Aphosphatase, active towards phosphorylase a and phosphorylated proteins casein and histone II-A , was isolated from Saccharomyces cerevisiae 257. The enzyme dephosphorylated glycogen phosphorylase from commercial yeast rendering it inactive. The protein phosphatase activity was not influenced by any metal ions. Phosphorylase phosphatase activity was slightly stimulated by p -nitrophenyl phosphate and inhibited by heparin.

• Publication year

  1998

• Venue

  Zeitschrift für Naturforschung C - A Journal of Biosciences

• Publication date

  1998-12-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1515/znc-1998-11-1203PMID 9933962
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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