Abstract
Homogeneous glycogen synthetase b has been obtained from both trout liver and rat liver. A molecular weight in the range of 260,000 was obtained for the enzyme from both sources. The trout enzyme appears to have less affinity for homologous glycogen than the rat enzyme as evidenced by the lesser fraction of the former which sediments with the glycogen pellet and by the dissociation of the glycogen-enzyme complex from the former but not the latter on DEAE-cellulose columns. A subunit molecular weight of 85,000 was determined for the rat enzyme, suggesting that it exists as a trimer. Further aggregation to a component of twice the original size occurs on storage in the cold. Determinations of alkali-labile phosphate and reactive sulfhydryl groups gave values of 12.4 and about 6, respectively. Activity decreased linearly to zero with the titration of the first 3 sulfhydryl groups (or the first 2 when glycogen was present), indicating that at least one of the most reactive groups is essential for activity. Incubation of the purified synthetase at 0° led to inactivation which was reversed on rewarming. Glycogen protected against this cold inactivation. Homogeneous rat liver synthetase b serves as a substrate for synthetase phosphatase which is currently being purified.
Supported by a grant (AM-08873) from the National Institutes of Health.
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Abbreviations
- cAMP:
-
cyclic adenosine 3′, 5′-phosphate
- UDPG:
-
UDP-glucose
- G-6-P:
-
glucose 6-phosphate
- SDS:
-
sodium dodecyl sulfate
- DTNB:
-
5, 5′-dithiobis (2-nitrobenzoic acid)
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Segal, H.L., Lin, D.C. (1974). Liver Glycogen Synthetase. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_8
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DOI: https://doi.org/10.1007/978-3-642-80817-3_8
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