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The presence of glycogen synthase in phosphorylase kinase preparations isolated from rabbit skeletal muscles

Shur, S.A.; Skolysheva, L.K.; Vul'fson, P.L.

Biokhimiia 51(9): 1446-1453

1986

ISSN/ISBN: 0320-9725
PMID: 3094592
Document Number: 270830
Phosphorylase kinase isolated from rabbit skeletal muscle contains a protein whose molecular mass as determined by polyacrylamide gel electrophoresis is 571 000 Da. The protein was found to possess a higher affinity for glycogen as compared to phosphorylase kinase and phosphorylase. The protein separated from kinase by chromatography on a DEAE-cellulose column produced during SDS electrophoresis one protein band corresponding to Mr of 95 200 Da. The above properties of the protein and the glycogen synthetase activity revealed in the presence of glucose-6-phosphate suggest that phosphorylase kinase preparations contain a hexameric form of glycogen synthetase.

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