Subcellular Location of Semicarbazide‐Sensitive Amine Oxidase in Rat Aorta
- 1 November 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 112 (1), 87-94
- https://doi.org/10.1111/j.1432-1033.1980.tb04990.x
Abstract
With tyramine as a 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.This publication has 29 references indexed in Scilit:
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