ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract— Monoamine oxidase was purified approximately 40-fold from beef brain mitochondria. The purification procedure involved extraction with a non-ionic detergent (Nonion NS-210) after heat treatment, ammonium sulphate fractionation, chromatographies on DEAE-cellulose and Sepharose 6B, and a continuous flow electrophoresis. A major component (enzyme 1) with a higher specific activity and a minor component (enzyme 2) with a lower specific activity were separated. Properties of both enzymes towards kynuramine including pH-optimum and Km values were similar, but the enzyme 1 had the higher specific activity towards tyramine whereas that of enzyme 2 was towards normetane-phrine. Fluorescence spectra indicated that the enzyme 1 is a flavoprotein. Copper was not detected, and copper chelating agents did not inhibit the enzyme. p-Chloromercuribenzoate and JV-ethylmaleimide inhibited the enzyme, indicating the presence of the essential SH-groups.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1971.tb11986.x
