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The permeability of the lysosomal membrane to small ions.
The permeability of the lysosomal membrane to small anions and cations was studied at 37 degrees C and pH 7.0 in a lysosomal-mitochondrial fraction isolated from the liver of untreated rats. TheExpand
Active proton uptake by chromaffin granules: observation by amine distribution and phosphorus-31 nuclear magnetic resonance techniques.
The hydrogen ion activity within isolated chromaffin granules can be estimated from the distribution of the weak base methylamine and from phosphorus-31 nuclear magnetic resonance spectra of ATPExpand
Dicyclohexylcarbodiimide binds specifically and covalently to cytochrome c oxidase while inhibiting its H+-translocating activity.
We have investigated the covalent binding of dicyclohexylcarbodiimide (DCCD) to cytochrome c oxidase in relation to its inhibition of ferrocytochrome c-induced H+ translocation by the enzymeExpand
The effect of N,N'-dicyclohexylcarbodiimide on enzymes of bioenergetic relevance.
The oxidation of exogenous cytochrome c by mitochondria
Several reports in the past have dealt with the oxidation of cytochrome c added to suspensions of rat liver mitochondria. Yet, it is generally believed that the cytochrome cannot penetrate the outerExpand
Membrane reconstitution of the energy-conserving enzymes of oxidative phosphorylation.
  • R. Casey
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 17 December 1984
Use of N,N'-dicyclohexylcarbodiimide to study membrane-bound enzymes.
Publisher Summary The use of N,N´-dicyclohexylcarbodiimide (DCCD) to study membrane-bound enzymes started with the observation that DCCD strongly inhibits the proton-translocating adenosineExpand
Studies on the molecular basis of H+ translocation by cytochromec oxidase
We report here studies which characterize further the interaction ofN,N′-dicyclohexylcarbodiimide with cytochromec oxidase leading to inhibition of H+ translocation by the enzyme. Further evidence isExpand
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