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

Shinri Tamura; Yoichi Suzuki; Kunimi Kikuchi; Shigeru Tsuiki

doi:10.1016/0006-291X(86)91078-8

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

Shinri Tamura, Yoichi Suzuki, Kunimi Kikuchi, Shigeru Tsuiki

Tohoku Medical Megabank Organization (ToMMo)

Research output: Contribution to journal › Article › peer-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 M_r = 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 language	English
Pages (from-to)	212-218
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	140
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(86)91078-8
Publication status	Published - 1986 Oct 15

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(86)91078-8

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

@article{05679a3112654d40918e7c276d1eacd3,

title = "Identification and characterization of Mg2+-dependent phosphotyrosyl protein phosphatase from rat liver cytosol",

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.",

author = "Shinri Tamura and Yoichi Suzuki and Kunimi Kikuchi and Shigeru Tsuiki",

year = "1986",

month = oct,

day = "15",

doi = "10.1016/0006-291X(86)91078-8",

language = "English",

volume = "140",

pages = "212--218",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "1",

}

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

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.

UR - http://www.scopus.com/inward/record.url?scp=0022930396&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022930396&partnerID=8YFLogxK

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 -