Partial purification of pig aorta amine oxidases.
Two amine oxidases have been partially purified from pig aorta and their porperties investigated: one is similar to pig plasma oxidase (benzylamine oxidase), the other to lysyloxidase. Both are inhibited by carbonyl reagents and cupric copper chelating agents, but they strongly differ in the kinetic properties. The benzylamine oxidase has a maximal reaction rate at acid pH values, the lysyloxidase has an optimum around pH 6.8.
Partial purification of pig aorta amine oxidases. Two amine oxidases have been partially purified from pig aorta and their porperties investigated: one is similar to pig plasma oxidase (benzylamine oxidase), the other to lysyloxidase. Both are inhibited by carbonyl reagents and cupric copper chelating agents, but they strongly differ in the kinetic properties. The benzylamine oxidase has a maximal reaction rate at acid pH values, the lysyloxidase has an optimum around pH 6.8.