Subcellular localization and ionic properties of acetyl-coenzyme A synthetase in the electric organ of Torpedo marmorata

  • Morot-Gaudry Y
  • Diebler M
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Acetyl-CoA synthetase activity was shown to be present in pure cholinergic synaptosomes from electric organ of Torpedo marmorata. After osmotic disruption of synaptosomes a substantial part of the activity was recovered in the soluble fraction. The effects of varying pH and increasing K+ concentrations on the synaptosomal enzyme activity were shown to differ from those observed with the mitochondrial enzyme. Whereas this latter enzyme showed optimal activity above pH 8.5, and a maximal activation in the presence of 120 mM-K+, the synaptosomal enzyme exhibited an optimal activity at pH 7.9 and a moderate K+ stimulatory effect with an optimal concentration of 30 mM.

Author-supplied keywords

  • Acetate-CoA Ligase/*metabolism
  • Animal
  • Coenzyme A Ligases/*metabolism
  • Electric Organ/drug effects/*enzymology
  • Fishes/*metabolism
  • Hydrogen-Ion Concentration
  • In Vitro
  • Potassium/pharmacology
  • Sodium/pharmacology
  • Subcellular Fractions/drug effects/enzymology

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  • Y Morot-Gaudry

  • M F Diebler

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