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Department of Physiological Sciences, School of Veterinary Medicine, University of California, Davis, California 95616
The activities of phosphohexose isomerase, pyruvate kinase, L-
-glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, malic enzyme, dihydroxyacetone kinase and hexose phosphorylating capacity were measured in ad libitum-fed rats, starved rats, and starved rats refed for 1, 2 and 3 days. The activities of all enzymes measured increased to about twice the level measured in rats adapted to ad libitum feeding on days 2 and 3 of refeeding, except the activity of L-
-glycerophosphate dehydrogenase and the hexose phosphorylating capacity, which after the overshoot at 2 days returned to normal levels 3 days after refeeding. Treatment with 8-azaguanine resulted in high levels of liver glycogen and prevented the overshoot in enzyme activities but not the increase back to normal levels. Phosphorylase activity was the same in both treated and nontreated rats; thus, increased liver glycogen levels in rats treated with azaguanine could not be explained on the basis of phosphorylase activity. 8-Azaguanine did decrease food intake; however, the overshoot was also observed in pair-fed rats. Therefore, the absence of overshoot in azaguanine-treated rats was not due to a decrease in food intake. The observed overshoot in enzyme activities on day 2 of refeeding was not observed in rats which received the first injection of the antibiotic 12 hours after refeeding. A possible explanation of the data is that the overshoot observed after refeeding is dependent on de novo RNA synthesis which occurs at least 12 hours after refeeding.
Manuscript received 1 July 1969.