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 |
|---|---|
| Pages (from-to) | 1349-1356 |
| Number of pages | 8 |
| Journal | Biochemistry |
| Volume | 15 |
| Issue number | 6 |
| State | Published - Dec 1 1976 |
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ASJC Scopus subject areas
- Biochemistry
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Purification and properties of rabbit-liver glycogen synthase. / Killilea, S. Derek; Whelan, William J.
In: Biochemistry, Vol. 15, No. 6, 01.12.1976, p. 1349-1356.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and properties of rabbit-liver glycogen synthase
AU - Killilea, S. Derek
AU - Whelan, William J.
PY - 1976/12/1
Y1 - 1976/12/1
N2 - 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.
AB - 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.
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M3 - Article
C2 - 814926
AN - SCOPUS:0017260855
VL - 15
SP - 1349
EP - 1356
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 6
ER -