An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues

Philip Cohen; Susanne Klumpp; Donald L. Schelling

doi:10.1016/0014-5793(89)80803-8

An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues

Philip Cohen
, Susanne Klumpp
, Donald L. Schelling

Research output: Contribution to journal › Article › peer-review

468 Citations (Scopus)

Abstract

The type 2A protein phosphatases in mammalian tissue extracts are inhibited completely and specifically by 1-2 nM okadaic acid. In contrast, type 1 protein phosphatases are hardly affected at these concentrations, complete inhibition requiring 1 μM okadaic acid. These observations have been exploited to develop an improved procedure for the identification and quantitation of type 1, type 2A and type 2C protein phosphatases in tissue extracts.

Original language	English
Pages (from-to)	596-600
Number of pages	5
Journal	FEBS Letters
Volume	250
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(89)80803-8
Publication status	Published - 3 Jul 1989

Keywords

Inhibitor protein
Okadaic acid
Protein phosphatase
Protein phosphorylation
Tumor promoter

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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Cite this

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title = "An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues",

abstract = "The type 2A protein phosphatases in mammalian tissue extracts are inhibited completely and specifically by 1-2 nM okadaic acid. In contrast, type 1 protein phosphatases are hardly affected at these concentrations, complete inhibition requiring 1 μM okadaic acid. These observations have been exploited to develop an improved procedure for the identification and quantitation of type 1, type 2A and type 2C protein phosphatases in tissue extracts.",

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AU - Cohen, Philip

AU - Klumpp, Susanne

AU - Schelling, Donald L.

PY - 1989/7/3

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N2 - The type 2A protein phosphatases in mammalian tissue extracts are inhibited completely and specifically by 1-2 nM okadaic acid. In contrast, type 1 protein phosphatases are hardly affected at these concentrations, complete inhibition requiring 1 μM okadaic acid. These observations have been exploited to develop an improved procedure for the identification and quantitation of type 1, type 2A and type 2C protein phosphatases in tissue extracts.

AB - The type 2A protein phosphatases in mammalian tissue extracts are inhibited completely and specifically by 1-2 nM okadaic acid. In contrast, type 1 protein phosphatases are hardly affected at these concentrations, complete inhibition requiring 1 μM okadaic acid. These observations have been exploited to develop an improved procedure for the identification and quantitation of type 1, type 2A and type 2C protein phosphatases in tissue extracts.

KW - Inhibitor protein

KW - Okadaic acid

KW - Protein phosphatase

KW - Protein phosphorylation

KW - Tumor promoter

UR - https://www.scopus.com/pages/publications/0024361302

U2 - 10.1016/0014-5793(89)80803-8

DO - 10.1016/0014-5793(89)80803-8

M3 - Article

C2 - 2546812

AN - SCOPUS:0024361302

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VL - 250

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EP - 600

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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