McGowan R E, Muir R M
Botany Department, The University of Iowa, Iowa City, Iowa 52240.
Plant Physiol. 1971 May;47(5):644-8. doi: 10.1104/pp.47.5.644.
A procedure has been developed for the purification of amine oxidase (E.C. 1.4.3.4) from etiolated pea epicotyls (Pisum sativum cv. Little Marvel). The enzyme is sensitive to copper chelating reagents and carbonyl reagents, but is not inhibited by sulfhydryl reagents. The purified enzyme has a molecular weight of 1.85 x 10(5), as determined by sedimentation equilibrium centrifugation, and has been shown to be specifically stimulated by phosphate.
已开发出一种从黄化豌豆上胚轴（豌豆品种小奇迹）中纯化胺氧化酶（E.C. 1.4.3.4）的方法。该酶对铜螯合剂和羰基试剂敏感，但不受巯基试剂抑制。通过沉降平衡离心法测定，纯化后的酶分子量为1.85×10⁵，并且已证明其受到磷酸盐的特异性刺激。
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