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Abstract
Fructose 1,6-bisphosphatse is an enzyme that plays an important physiological role, especially in the gluconeogenic tissues, as kidney-cortex. There are several mechanisms to guarantee a strict regulation of its activity. We will emphasize the importance of divalent cations as enzyme effectors, leaving aside their role as catalytic ions. In this work we describe the kinetic characteristics of the purified enzyme from rat-kidney cortex, as a functions of the concentrations of the most important cations for the enzyme activity, magnesium and manganese.
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