Subcellular Location of Semicarbazide-sensitive Amine Oxidase in Rat Aorta

Wibo, Maurice;Duong, AT.;Godfraind, Theophile
(1980) European Journal of Biochemistry —

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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 semiicarbazide. 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.
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Wibo, M., Duong, AT., & Godfraind, T. (1980). Subcellular Location of Semicarbazide-sensitive Amine Oxidase in Rat Aorta. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1980.tb04990.x