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


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Wolfman, NM; Hammes, GG

Published Date

  • December 25, 1979

Published In

Volume / Issue

  • 254 / 24

Start / End Page

  • 12289 - 12290

PubMed ID

  • 40994

Pubmed Central ID

  • 40994

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States