Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40

Alan M. Mahrenholz, Philip Votaw, Peter Roach, Anna De Paoli-Roach, Thomas F. Zioncheck, Marietta L. Harrison, Robert L. Geahlen

Research output: Contribution to journalArticle

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Abstract

Glycogen synthase from rabbit skeletal muscle was found to be phosphorylated by a protein-tyrosine kinase, p40, purified from bovine thymus. The phosphorylation, to a stoichiometry of 0.4-0.5 mol/mol subunit, was specific for a single tyrosine residue in the sequence EEDGERYDEDEE. This acidic sequence has considerable similarity to the site recognized by p40 in erythrocyte band 3 protein. In the analysis of the phosphorylated peptide, it was noted that the sequence -RY (P)- impeded cleavage by either trypsin or automatic Edman degradation.

Original languageEnglish
Pages (from-to)52-58
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume155
Issue number1
DOIs
StatePublished - Aug 30 1988

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Thymus
Glycogen Synthase
Phosphorylation
Protein-Tyrosine Kinases
Thymus Gland
Erythrocyte Anion Exchange Protein 1
Stoichiometry
Trypsin
Tyrosine
Muscle
Skeletal Muscle
Erythrocytes
Rabbits
Degradation
Peptides
adjuvant P40

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40. / Mahrenholz, Alan M.; Votaw, Philip; Roach, Peter; De Paoli-Roach, Anna; Zioncheck, Thomas F.; Harrison, Marietta L.; Geahlen, Robert L.

In: Biochemical and Biophysical Research Communications, Vol. 155, No. 1, 30.08.1988, p. 52-58.

Research output: Contribution to journalArticle

Mahrenholz, Alan M. ; Votaw, Philip ; Roach, Peter ; De Paoli-Roach, Anna ; Zioncheck, Thomas F. ; Harrison, Marietta L. ; Geahlen, Robert L. / Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40. In: Biochemical and Biophysical Research Communications. 1988 ; Vol. 155, No. 1. pp. 52-58.
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