PMID: 40994Dec 25, 1979

A calorimetric study of the interaction of ATP with rabbit muscle phosphofructokinase

The Journal of Biological Chemistry
N M Wolfman, G G Hammes

Abstract

The heat of interaction of ATP with phosphofructokinase from rabbit muscle was determined at 25 degrees C in 0.1 M potassium phosphate, pH 7.0 and 8.0. The limiting value of the enthalpy change at high ATP concentrations was found to be -11.5 kcal mol of enzyme polypeptide chains. Since phosphate and imidazole have very different heats of ionization (+0.8 and +7.5 kcal/mol, respectively), this suggests that the binding of at least two protons to the enzyme occurs concomitantly with the binding of ATP at the regulatory site.

Related Concepts

Adenosine Triphosphate, Chromium Ammonium Salt
Calorimetry
Hydrogen-Ion Concentration
Muscle
6-Phosphofructokinase

Related Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.