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 language | English (US) |
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Pages (from-to) | 1349-1356 |
Number of pages | 8 |
Journal | Biochemistry |
Volume | 15 |
Issue number | 6 |
DOIs | |
State | Published - Mar 1 1976 |
ASJC Scopus subject areas
- Biochemistry