1976
DOI: 10.1016/0026-0495(76)90159-1
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Regulation of rat liver glycogen synthesis and activities of glycogen cycle enzymes by glucose and galactose

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1976
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Cited by 33 publications
(26 citation statements)
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“…When the combination of glucose, galactose, and insulin was added to the perfusate, synthetase was not only activated 10-fold, but also the degree of activation was proportional to perfusate glucose concentration. This is qualitatively similar to the glucose concentration dependence observed in the adult rat liver perfused under similar conditions (28), and this concentration dependence of synthetase activation may be important for the rapid synthesis of glycogen during feeding.…”
Section: Discussionsupporting
confidence: 84%
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“…When the combination of glucose, galactose, and insulin was added to the perfusate, synthetase was not only activated 10-fold, but also the degree of activation was proportional to perfusate glucose concentration. This is qualitatively similar to the glucose concentration dependence observed in the adult rat liver perfused under similar conditions (28), and this concentration dependence of synthetase activation may be important for the rapid synthesis of glycogen during feeding.…”
Section: Discussionsupporting
confidence: 84%
“…Although it is generally assumed (1, 23) that galactose is metabolized to glycogen in infants, both increased and decreased liver glycogen levels have been observed after large galactose feedings in adults (3,14). In a recent study using the isolated perfused adult rat liver, we demonstrated increased liver glycogen after perfusion with galactose (28). We also noted that galactose regulated the activities of glycogen synthetase and phosphorylase.…”
Section: Discussionsupporting
confidence: 50%
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