There was an increase in copper content proportional to the increase in specific activity of the enzyme during the purification of amine oxidase of Aspergillus niger. The recrystal-lized enzyme preparation contained 1 g atom of copper per 83, 000 g of protein. This in-dicated that the enzyme contained 3 g atoms of copper per mole of enzyme. The copper in the enzyme was removed by dialysis against sodium diet hyldithiocarbamate with con-comitant loss of activity. The dialyzed enzyme was reactivated by the addition of cupric copper.
The copper in the enzyme was present in cupric state. No valency change of the copper was observed in the catalytic activity.
The enzyme was inhibited by various chelating agents, and potently inhibited by various carbonyl reagents.

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