Abstract
Glucagon (250 microgram/kg body wt.) intravenously injected into normal fed rats produces within 5 min a marked inactivation of liver phosphofructokinase, only observed when the enzyme activity is measured at subsaturating concentrations of fructose 6-phosphate. Since half-maximal inactivation is observed at a dose of glucagon of 0.32 microgram/body wt., a dose within the range of the physiological concentrations of the hormone, the inactivation of phosphofructokinase can occur in vivo in response to physiological changes in the concentration of glucagon. In gluconeogenic conditions (starved rats or high-protein-diet-fed rats), there is a marked inactivation of liver phosphofructokinase at subsaturating concentrations of fructose 6-phosphate similar to that found in normal fed rats after glucagon treatment. In these gluconeogenic conditions a 50% decrease in the Vmax. of the enzyme is also observed. No significant changes in phosphofructokinase activity either at subsaturating concentrations of fructose 6-phosphate or in the Vmax. of the enzyme are observed when rats are fed on a high-carbohydrate diet. In the last dietary condition, glucagon treatment produces similar effects to that described in the normal fed rats. Similar results have been obtained in the above condtions for pyruvate kinase L activity when measured at subsaturating concentrations of phosphoenolpyruvate.
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