On the expected relationship between Gibbs energy of ATP hydrolysis and muscle performance

Biophys Chem. 1995 Apr;54(2):137-42. doi: 10.1016/0301-4622(94)00129-8.

Abstract

Allowing for creatine kinase buffering of changes in adenine nucleotide concentrations, and the known relationship between muscle performance and rate of ATP hydrolysis by myosin, the variation of exerted force with intracellular Gibbs energy of ATP hydrolysis is calculated for voluntary muscle contraction. The resulting relationship is sigmoidal, most of the operating range coinciding with the quasi-linear range around the inflection point. Finger-flexor muscle magnetic resonance spectroscopy data are shown to be in line with this prediction.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Energy Metabolism
  • Humans
  • Hydrolysis
  • Magnetic Resonance Spectroscopy
  • Mathematical Computing
  • Muscle Contraction / physiology
  • Muscle, Skeletal / metabolism*
  • Muscle, Skeletal / physiology*
  • Rats
  • Thermodynamics

Substances

  • Adenosine Diphosphate
  • Adenosine Triphosphate