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

Biochem Biophys Res Commun. 1988 Aug 30;155(1):52-8. doi: 10.1016/s0006-291x(88)81048-9.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Glycogen Synthase / isolation & purification
  • Glycogen Synthase / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Phosphopeptides / isolation & purification
  • Phosphorylation
  • Protein-Tyrosine Kinases / physiology*
  • Rabbits
  • Thymus Gland / enzymology*

Substances

  • Phosphopeptides
  • Glycogen Synthase
  • Protein-Tyrosine Kinases