Abstract
The administration of carbohydrate elicits a rapid increase of rat liver ATP d-hexose 6-phosphotransferase when this enzyme activity has been decreased by feeding a high-fat, carbohydrate-free diet for several days. Several monosaccharides were tested for their ability to induce the increase of phosphotransferase. The results indicate a preferential response of this enzyme to glucose as compared to other very closely related sugars. The administration of puromycin and actinomycin prevents the response, and suggests a de novo synthesis of protein to explain the increase in enzyme activity caused by carbohydrate. The administration of high doses of commercial insulin to intact animals increases slightly the activity of phosphotransferase already decreased by a carbohydrate-free diet. It appears that a minimum amount of circulating insulin as well as a certain level of glucose in the liver are necessary to maintain adequate enzyme activities. The adrenal glands do not seem to be essential for the induction of phosphotransferase; nevertheless, hydrocortisone seemed to facilitate the inductive effect of exogenous glucose.
Published Version
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