A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis

Clara R. Krisman, Roberto A. Geremia, William J. Whelan

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4 Scopus citations


A macromolecular (1→4)-α-d-[14C]glucan-protein complex was synthesized with a rat liver preparation and uridine diphosphate d-[14C]glucose. The size of the complex is contributed by both the protein and the (1→4)-α-d-glucosyl-oligomer components. Iodoacetamide treatment did not change the migration properties on Bio-Gel A-50m. Therefore, disulfide bonds linking glucan-protein subunits seem not to be involved. The [14C]glucan-protein, precipitated by diluted trichloroacetic acid, was digested by α-amylase, phosphorylase a, and proteases. The extent of proteolysis was greater for a complex having fewer d-glucose units incorporated. After proteolytic digestion of that complex, the labeled fragments behaved on electrophoresis, and ion-exchange and gel chromatography as [14C]glucosylated peptides. These findings support previous conclusions that the primer for liver glycogen synthesis is a protein on which glycogen is built up by covalent attachment.

Original languageEnglish (US)
Pages (from-to)35-45
Number of pages11
JournalCarbohydrate Research
Issue number1
StatePublished - Jun 1 1986

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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