Purification and Properties of Rabbit-Liver Glycogen Synthase

S. Derek Killilea, William J. Whelan

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Glycogen synthase b was purified from rabbit liver by a procedure involving isolation of the glycogen-enzyme complex, DEAE-cellulose chromatography, and affinity chromatography. The purified enzyme had a specific activity of 25 μmol of glucose transferred from UDPglucose into glycogen per min per mg of protein at 30°C in the presence of 10 mM glucose 6-P, and appeared to be homogeneous by the criterion of polyacrylamide disc gel electrophoresis. The b form was convertible into the a form by a rabbit-liver protein phosphatase. A subunit size of 85 000 was determined by electrophoresis in sodium dodecyl sulfate and molecular weights of 183 000 ± 20 000 and 170 000 ± 21 000 were determined for the a and b forms of the enzyme, respectively. On conversion of the a into the b form, 1.13 mol of phosphate was incorporated per 85 000 g of protein. The degree of phosphorylation and loss of glycogen synthase a activity paralleled each other.

Original languageEnglish (US)
Pages (from-to)1349-1356
Number of pages8
JournalBiochemistry
Volume15
Issue number6
DOIs
StatePublished - Mar 1 1976

ASJC Scopus subject areas

  • Biochemistry

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