Abstract

1. 1. For the determination of relationship between FDP and ATP in the rat liver pyruvate kinase regulation, kinelic studies have been carried out at several ATP and FDP concentrations. 2. 2. The results obtained on FDP activation show a great cooperativity for FDP saturation with a Hill coefficient of h = 2.79. 3. 3. Kinetic studies on ATP inhibition also show a great cooperativity for ATP saturation ( h = 2.84) at high FDP concentrations. 4. 4. These results may contribute to explain the regulation of rat liver pyruvate kinase accounting for the activity of this enzyme at high FDP concentrations modulated by small changes in ATP concentrations.

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