Appearance of a nonfunctional isozyme of hepatic glycogen synthase in late gestation

Stephen D. Hsu, Stephen R. Jaspers, Betty B. Davis, Robert R. Cardell, Thomas B. Miller, Richard L. Drake

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Glycogen levels, glycogen synthase activities, and glycogen synthase protein levels were determined in liver tissues obtained from 14- to 19-day-old fetal mice, newborn mice, and adult mice. The results of these experiments demonstrate a significant increase in the quantity of hepatic glycogen synthase beginning at Day 17 of gestation and reaching adult levels at birth. However, during the same time period, there is a dramatic decrease in total glycogen synthase activity suggesting that the accumulating glycogen synthase molecules are unable to transfer UDP-glucose to glycogen. These inversely coordinated changes in the quantity and activity of glycogen synthase are consistent with the suggestion that glycogen synthesis in the near-term fetal mouse is being maintained by preexisting enzyme, while accumulating enzyme molecules may represent a quiescent isozyme.

Original languageEnglish (US)
Pages (from-to)152-156
Number of pages5
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Aug 15 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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