A new method for purification of soluble benzylamine oxidase from bovine aorta with specific activity of more than 100 units is described. The optical and magnetic properties of the enzyme have been studied. The enzyme contains type II copper, the environment of which is sensitive to pH, substrate, inhibitors and chelators. An addition of substrate and inhibitors results in a formation of free radicals on the enzyme. The properties of the enzyme are compared to those of copper-containing amine oxidases from other sources.