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Title: Regulation of rat-renal cortex phosphofructokinase activity by pH. Author: Sola MM, Salto R, Oliver FJ, Gutiérrez M, Vargas AM. Journal: Enzyme Protein; 1993; 47(2):99-104. PubMed ID: 8193676. Abstract: The activity of phosphofructokinase purified from rat kidney cortex has been assayed at two different pH values. At pH 7 the enzyme showed cooperativity for the binding of fructose 6-phosphate (Fru-6-P) and a strong allosteric inhibition by ATP. When the assays were done at pH 8 hyperbolic kinetics were observed for both substrates, a smaller inhibition by ATP was observed and the Vmax for ATP and for Fru-6-P was higher than at pH 7. A sequential reaction mechanism was inferred. Results are discussed in terms of the importance of a reduced hexose-phosphate cycling rate during metabolic acidosis induced by exercise.[Abstract] [Full Text] [Related] [New Search]