Buffoni F, Marino P, Pirisino R
Ital J Biochem. 1976 May-Jun;25(3):191-203.
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.
已从猪主动脉中部分纯化出两种胺氧化酶,并对其性质进行了研究:一种类似于猪血浆氧化酶(苄胺氧化酶),另一种类似于赖氨酰氧化酶。两者均受羰基试剂和铜螯合剂抑制,但在动力学性质上有很大差异。苄胺氧化酶在酸性pH值下有最大反应速率,赖氨酰氧化酶在pH 6.8左右有最佳活性。