Identification and characterization of Mg2+-dependent phosphotyrosyl protein phosphatase from rat liver cytosol

Shinri Tamura, Yoichi Suzuki, Kunimi Kikuchi, Shigeru Tsuiki

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Although highly purified preparations of Mg2+-dependent phosphoseryl protein phosphatase (also designated phosphatase IA or phosphatase 2C) dephosphorylated phosphotyrosyl histone, the activity has been resolved from phosphatase IA by polyacrylamide gel electrophoresis at pH 9.5. This novel phosphotyrosyl-specific protein phosphatase absolutely requires Mg2+ or Mn2+ for activity, is inhibited by Zn2+, vanadate and fluoride, and has an optimal pH of 9.0 and Mr = 50,000. Certain properties of this phosphatase so closely resemble those of phosphatase IA that the two enzymes tend to be copurified through various separation procedures.

Original languageEnglish
Pages (from-to)212-218
Number of pages7
JournalBiochemical and biophysical research communications
Volume140
Issue number1
DOIs
Publication statusPublished - 1986 Oct 15

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Identification and characterization of Mg<sup>2+</sup>-dependent phosphotyrosyl protein phosphatase from rat liver cytosol'. Together they form a unique fingerprint.

Cite this