Purification and properties of rabbit-liver glycogen synthase

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Abstract
Glycogen synthase b (EC 2.4.1.11) 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 .mu.mol of glucose transferred from UDPglucose into glycogen/min per mg of protein at 30.degree. C in the presence of 10 mM glucose 6-phosphate 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.

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