Subcellular location of semicarbazide-sensitive amine oxidase in rat aorta

Eur J Biochem. 1980 Nov;112(1):87-94. doi: 10.1111/j.1432-1033.1980.tb04990.x.

Abstract

With tyramine as substrate, a considerable part of the amine oxidase activity of rat aorta was inhibited by 0.1 mM semicarbazide. The residual activity was little affected by 1 mM semicarbazide. Oxidation of 5-hydroxytryptamine was not inhibited by 0.1 mM semicarbazide. The subcellular location of the semicarbazide-sensitive and semicarbazide-resistant amine oxidases was investigated by analytical density gradient centrifugation. The semicarbazide-resistant enzyme was identified with the mitochondrial monoamine oxidase, located in the outer envelope of mitochondria. The semicarbazide-sensitive amine oxidase was ascribed to the plasma membrane because it was distributed like 5'-nucleotidase and (oligomycin-insensitive) Mg2+-ATPase in various fractionation experiments, and markedly shifted by digitonin towards higher equilibrium densities in sucrose gradient.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aorta / enzymology*
  • Cell Membrane / enzymology
  • Centrifugation, Density Gradient
  • Digitonin / pharmacology
  • Female
  • Mitochondria, Muscle / enzymology
  • Monoamine Oxidase
  • Oxidoreductases Acting on CH-NH Group Donors / antagonists & inhibitors
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Rats
  • Semicarbazides / pharmacology*
  • Subcellular Fractions / enzymology

Substances

  • Semicarbazides
  • Monoamine Oxidase
  • Oxidoreductases Acting on CH-NH Group Donors
  • Digitonin