Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

Greg Moorhead; Carol MacKintosh; Nick Morrice; Philip Cohen

doi:10.1016/0014-5793(95)00197-H

Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

Greg Moorhead
, Carol MacKintosh
, Nick Morrice
, Philip Cohen

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

82 Scopus citations

Abstract

The form of protein phosphatase-1 associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration. The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the α and β isoforms) complexed to a 33 kDa glycogen-binding (G_L) subunit. The G_L subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.

Original language	English
Pages (from-to)	101-105
Number of pages	5
Journal	FEBS Letters
Volume	362
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(95)00197-H
State	Published - 3 Apr 1995
Externally published	Yes

Keywords

Glycogen
Glycogen synthase
Microcystin
Phosphorylase
Protein phosphatase

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10.1016/0014-5793(95)00197-H

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title = "Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography",

abstract = "The form of protein phosphatase-1 associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration. The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the α and β isoforms) complexed to a 33 kDa glycogen-binding (GL) subunit. The GL subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.",

keywords = "Glycogen, Glycogen synthase, Microcystin, Phosphorylase, Protein phosphatase",

author = "Greg Moorhead and Carol MacKintosh and Nick Morrice and Philip Cohen",

year = "1995",

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doi = "10.1016/0014-5793(95)00197-H",

language = "English",

volume = "362",

pages = "101--105",

journal = "FEBS Letters",

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T1 - Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

AU - Moorhead, Greg

AU - MacKintosh, Carol

AU - Morrice, Nick

AU - Cohen, Philip

PY - 1995/4/3

Y1 - 1995/4/3

N2 - The form of protein phosphatase-1 associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration. The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the α and β isoforms) complexed to a 33 kDa glycogen-binding (GL) subunit. The GL subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.

AB - The form of protein phosphatase-1 associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration. The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the α and β isoforms) complexed to a 33 kDa glycogen-binding (GL) subunit. The GL subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.

KW - Glycogen

KW - Glycogen synthase

KW - Microcystin

KW - Phosphorylase

KW - Protein phosphatase

UR - https://www.scopus.com/pages/publications/0028929093

U2 - 10.1016/0014-5793(95)00197-H

DO - 10.1016/0014-5793(95)00197-H

M3 - Article

C2 - 7720853

AN - SCOPUS:0028929093

SN - 0014-5793

VL - 362

SP - 101

EP - 105

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

Abstract

Keywords

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