Phosphorylation of glycogen synthase in isolated rabbit hepatocytes

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Specific antibodies were used to purify glycogen synthase from isolated rabbit hepatocytes that had been incubated in a medium containing [32P]phosphate. The enzyme gave rise to two main 32P-labeled CNBr fragments of electrophoretic mobilities similar to those obtained after phosphorylation of the enzyme by individual protein kinases in vitro.

Original languageEnglish
Pages (from-to)261-263
Number of pages3
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume804
Issue number2
DOIs
StatePublished - Jun 19 1984

Fingerprint

Glycogen Synthase
Hepatocytes
Phosphorylation
Rabbits
Enzymes
Protein Kinases
Phosphates
Antibodies
In Vitro Techniques

Keywords

  • (Rabbit hepatocyte)
  • Glycogen synthase
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Phosphorylation of glycogen synthase in isolated rabbit hepatocytes. / Ciudad, Carlos; De Paoli-Roach, Anna; Roach, Peter.

In: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 804, No. 2, 19.06.1984, p. 261-263.

Research output: Contribution to journalArticle

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