Comparison of the Properties of Semipurified Mitochondrial and Cytosolic Monoamine Oxidases from Rat Brain

C. S K Mayanil, N. Z. Baquer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Abstract: Mitochondrial and cytosolic monoamine oxidases were purified 220‐ and 129‐fold, respectively, from rat brain. The purification procedure involved extraction (without the use of detergents for mitochondrial monoamine oxidase), ammonium sulfate precipitation, and chromatography on Sephadex G‐25 and a DEAE‐cellulose column. The properties of both enzymes with kynuramine as substrate, including Km values and pH optima at different kynuramine concentrations; the Rf values on polyacrylamide gel electrophoresis; and the thermal in‐activation patterns were different. 2‐Mercaptoethanol, together with heat treatment, released the flavin and decreased the enzyme activity differentially for the two enzymes. The absorption spectrum showed a “Red shift” in the absorption maxima when the spectra of the non‐Triton‐treated purified preparations were compared with those of the Triton‐treated ones, thus possibly revealing that the mitochondrial and the cytosolic monoamine oxidases may be two different enzyme entities.

Original languageEnglish (US)
Pages (from-to)906-912
Number of pages7
JournalJournal of Neurochemistry
Volume43
Issue number4
DOIs
StatePublished - Jan 1 1984

Keywords

  • Cytosolic monoamine oxidase
  • Mitochondrial monoamine oxidase
  • Monoamine oxidase

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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