[Rotenone-sensitive oxidation of NADH and F0F1-ATPase activity in a homogenate of rat skeletal muscles during thermal adaptation]

Biokhimiia. 1993 Nov;58(11):1779-87.
[Article in Russian]

Abstract

A method has been developed for measuring the rates of rotenone-sensitive oxidation of NADH and oligomycin-sensitive hydrolysis of ATP in rat skeletal muscle homogenates. The method is based on the use of alamethicin which increases the permeability of the inner mitochondrial membrane for NADH and ATP. It has been shown that prolonged cold adaptation of rats (4 weeks, 4 degrees) does not change the activity of rotenone-sensitive NADH-oxidase in rat skeletal muscle homogenates which is equal to 12.4 +/- 4.4 nmol NADH/min/mg protein, but increases threefold that of F0F1-ATPase--from 31.8 +/- 7.4 up to 93.1 +/- 14.3 nmol P(i)/min/mg protein. It is suggested that prolonged cold adaptation induces structural-and-functional changes in the H(+)-ATP-synthetase complex of skeletal muscle mitochondria.

Publication types

  • English Abstract

MeSH terms

  • Adaptation, Physiological*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Cold Temperature
  • Intracellular Membranes / enzymology
  • Intracellular Membranes / metabolism
  • Male
  • Mitochondria, Muscle / enzymology
  • Mitochondria, Muscle / metabolism
  • Multienzyme Complexes / metabolism
  • Muscles / drug effects
  • Muscles / enzymology*
  • Muscles / physiology
  • NAD / metabolism*
  • NADH, NADPH Oxidoreductases / metabolism
  • Oligomycins / pharmacology
  • Oxidation-Reduction
  • Proton-Translocating ATPases / metabolism*
  • Rats
  • Rotenone / pharmacology*

Substances

  • Multienzyme Complexes
  • Oligomycins
  • Rotenone
  • NAD
  • Adenosine Triphosphate
  • NADH oxidase
  • NADH, NADPH Oxidoreductases
  • Proton-Translocating ATPases