title: Regulation of rat-renal cortex phosphofructokinase activity by pH.
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.
authors.affiliation: Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Granada, España.
authors.forename: M M
authors.initials: MM
authors.lastname: Sola
authors.forename: R
authors.initials: R
authors.lastname: Salto
authors.forename: F J
authors.initials: FJ
authors.lastname: Oliver
authors.forename: M
authors.initials: M
authors.lastname: Gutiérrez
authors.forename: A M
authors.initials: AM
authors.lastname: Vargas
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D000818:Animals; D005636:Fructosephosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
chemical_list: D005636:Fructosephosphates; C027618:fructose-6-phosphate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1