TY - JOUR
T1 - Identification and characterization of Mg2+-dependent phosphotyrosyl protein phosphatase from rat liver cytosol
AU - Tamura, Shinri
AU - Suzuki, Yoichi
AU - Kikuchi, Kunimi
AU - Tsuiki, Shigeru
N1 - Funding Information:
The authors are indebted to Mr. K. Konno and Mrs. C. Ito for their ful assistance. This work was supported by Grants-in-aid for scientific research from the Ministry of Education, Science and Culture, Japan.
PY - 1986/10/15
Y1 - 1986/10/15
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(86)91078-8
DO - 10.1016/0006-291X(86)91078-8
M3 - Article
C2 - 3022716
AN - SCOPUS:0022930396
VL - 140
SP - 212
EP - 218
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -