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The Purification and Properties of Rabbit Skeletal Muscle Glycogen Synthase.
- Source :
- European Journal of Biochemistry; Sep76 Part 1, Vol. 68 Issue 1, p21-30, 10p
- Publication Year :
- 1976
-
Abstract
- Glycogen synthase a was purified over 500-fold by a procedure which involved solubilisation of the enzyme from a protein-glycogen complex by the action of endogenous phosphorylase and debranching enzyme, followed by DEAE-cellulose chromatography, and either gel filtration on Sepharose 4B or fractionation with polyethylene glycol. 15 mg of protein could be obtained from 1000 g of muscle in five days, corresponding to a yield of 20%. The purity was over 90% as judged by gel electrophoresis and ultracentrifugal analysis. The amino acid composition was determined and the absorption coefficient, A<superscript>1%</superscript><subscript>280nm</subscript>, measured refractometrically was 13.4. Glycogen synthase a sedimented as two major components, both of which were enzymatically active. The smaller species (13.3S) comprised 85% and the larger species (19.0S) 15% of the material. The molecular weight of the 13.3-S component was determined to be 377000 by high-speed sedimentation equilibrium centrifugation. The subunit molecular weight measured by gel electrophoresis in the presence of sodium dodecylsulphate was 88000 indicating that the 13.3-S species is a tetramer. The properties of the enzyme are compared to those obtained by other workers. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 68
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13499966
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1976.tb10761.x