Multiple phosphorylation of mouse muscle glycogen synthase

Fook Thean Lee, Zafeer Ahmad, Anna De Paoli-Roach, Peter Roach

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Glycogen synthase was isolated from extracts of mouse diaphragm muscle by immunoprecipitation with specific antibodies raised against the rabbit muscle enzyme. A procedure was developed which permitted phosphorylation of the immunoprecipitated enzyme by several purified protein kinases. Peptide mapping techniques (including reverse-phase HPLC and thin-layer electrophoresis and chromatography) were used to compare tryptic phosphopeptides of the rabbit and mouse muscle enzymes. The results demonstrated a high degree of similarity in the chemical properties of these peptides, suggesting significant homology around the phosphorylation sites in these proteins. Thus, mouse peptides corresponding to the rabbit muscle peptides containing sites 1a, 1b, 2, 3, and 5 were identified, with protein kinase recognition specificities identical to those of the rabbit enzyme. The study indicates significant conservation in the muscle isozymes of glycogen synthase between mouse and rabbit as well as a similar distribution of phosphorylation sites throughout the enzyme subunit.

Original languageEnglish
Pages (from-to)615-620
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume258
Issue number2
DOIs
StatePublished - Nov 1 1987

Fingerprint

Glycogen Synthase
Phosphorylation
Muscle
Rabbits
Muscles
Enzymes
Peptides
Protein Kinases
Phosphopeptides
Peptide Mapping
Thin Layer Chromatography
Diaphragms
Chromatography
Diaphragm
Electrophoresis
Immunoprecipitation
Chemical properties
Isoenzymes
Conservation
High Pressure Liquid Chromatography

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Multiple phosphorylation of mouse muscle glycogen synthase. / Lee, Fook Thean; Ahmad, Zafeer; De Paoli-Roach, Anna; Roach, Peter.

In: Archives of Biochemistry and Biophysics, Vol. 258, No. 2, 01.11.1987, p. 615-620.

Research output: Contribution to journalArticle

@article{46256a5605f04231bb73675d811e4438,
title = "Multiple phosphorylation of mouse muscle glycogen synthase",
abstract = "Glycogen synthase was isolated from extracts of mouse diaphragm muscle by immunoprecipitation with specific antibodies raised against the rabbit muscle enzyme. A procedure was developed which permitted phosphorylation of the immunoprecipitated enzyme by several purified protein kinases. Peptide mapping techniques (including reverse-phase HPLC and thin-layer electrophoresis and chromatography) were used to compare tryptic phosphopeptides of the rabbit and mouse muscle enzymes. The results demonstrated a high degree of similarity in the chemical properties of these peptides, suggesting significant homology around the phosphorylation sites in these proteins. Thus, mouse peptides corresponding to the rabbit muscle peptides containing sites 1a, 1b, 2, 3, and 5 were identified, with protein kinase recognition specificities identical to those of the rabbit enzyme. The study indicates significant conservation in the muscle isozymes of glycogen synthase between mouse and rabbit as well as a similar distribution of phosphorylation sites throughout the enzyme subunit.",
author = "Lee, {Fook Thean} and Zafeer Ahmad and {De Paoli-Roach}, Anna and Peter Roach",
year = "1987",
month = "11",
day = "1",
doi = "10.1016/0003-9861(87)90384-5",
language = "English",
volume = "258",
pages = "615--620",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Multiple phosphorylation of mouse muscle glycogen synthase

AU - Lee, Fook Thean

AU - Ahmad, Zafeer

AU - De Paoli-Roach, Anna

AU - Roach, Peter

PY - 1987/11/1

Y1 - 1987/11/1

N2 - Glycogen synthase was isolated from extracts of mouse diaphragm muscle by immunoprecipitation with specific antibodies raised against the rabbit muscle enzyme. A procedure was developed which permitted phosphorylation of the immunoprecipitated enzyme by several purified protein kinases. Peptide mapping techniques (including reverse-phase HPLC and thin-layer electrophoresis and chromatography) were used to compare tryptic phosphopeptides of the rabbit and mouse muscle enzymes. The results demonstrated a high degree of similarity in the chemical properties of these peptides, suggesting significant homology around the phosphorylation sites in these proteins. Thus, mouse peptides corresponding to the rabbit muscle peptides containing sites 1a, 1b, 2, 3, and 5 were identified, with protein kinase recognition specificities identical to those of the rabbit enzyme. The study indicates significant conservation in the muscle isozymes of glycogen synthase between mouse and rabbit as well as a similar distribution of phosphorylation sites throughout the enzyme subunit.

AB - Glycogen synthase was isolated from extracts of mouse diaphragm muscle by immunoprecipitation with specific antibodies raised against the rabbit muscle enzyme. A procedure was developed which permitted phosphorylation of the immunoprecipitated enzyme by several purified protein kinases. Peptide mapping techniques (including reverse-phase HPLC and thin-layer electrophoresis and chromatography) were used to compare tryptic phosphopeptides of the rabbit and mouse muscle enzymes. The results demonstrated a high degree of similarity in the chemical properties of these peptides, suggesting significant homology around the phosphorylation sites in these proteins. Thus, mouse peptides corresponding to the rabbit muscle peptides containing sites 1a, 1b, 2, 3, and 5 were identified, with protein kinase recognition specificities identical to those of the rabbit enzyme. The study indicates significant conservation in the muscle isozymes of glycogen synthase between mouse and rabbit as well as a similar distribution of phosphorylation sites throughout the enzyme subunit.

UR - http://www.scopus.com/inward/record.url?scp=0023448626&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023448626&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(87)90384-5

DO - 10.1016/0003-9861(87)90384-5

M3 - Article

VL - 258

SP - 615

EP - 620

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -