Benzylamine oxidase from brain microvessels.

Copper-containing benzylamine oxidase with a specific activity of 200 units was isolated from bovine brain microvessels. It was shown that the content of the enzyme in microvessels was significantly higher as compared with large blood vessels such as heart aorta. Some physico-chemical properties of the enzyme were determined. The enzyme was inhibited by high concentrations of the substrate as well as thiol reagents and beta-aminopropionitrile fumarate. On the basis of EPR and optical spectra of the enzyme its copper was considered to be 'non-blue' type.