Affordable Access

Publisher Website

Phosphorylation site specificities of glycogen synthase kinases: Determination by peptide mapping using high-performance liquid chromatography

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
222
Issue
2
Identifiers
DOI: 10.1016/0003-9861(83)90550-7
Keywords
  • Regulation Of Metabolism And Of Enzyme Action
Disciplines
  • Biology

Abstract

Abstract A method is described which separates the various phosphorylation sites in glycogen synthase based on reverse phase high-performance liquid chromatography (HPLC) of tryptic 32P-peptides. Using this method we studied the phosphorylation site specificities of the kinases which act on glycogen synthase. The cAMP-dependent protein kinase phosphorylated sites 1a, 1b, and 2, whereas casein kinase II phosphorylated only site 5. Two calcium, calmodulin-dependent kinases, phosphorylase kinase and liver calmodulin-dependent synthase kinase, both phosphorylated site 2, and the latter enzyme also phosphorylated site 1b. A cAMP-independent kinase (kinase 4) purified from liver also specifically phosphorylated site 2. Synthase kinase 3 catalyzed the phosphorylation of only site 3. This HPLC method was also used to establish that all of these sites were subject to phosphorylation in vivo.

There are no comments yet on this publication. Be the first to share your thoughts.