Oosthuizen M M, van Wyk B, Schabort J C
Biochem Int. 1984 Dec;9(6):725-34.
Human plasma catalase and monoamine oxidase were purified for the first time to homogeneity. Monoamine oxidase purified 3200-fold with the aid of DEAE-Sepharose Cl-6B and Sepharose Cl-6B chromatography was devoid of catalase, aldehyde dehydrogenase and reductase activity. Homogeneous catalase was obtained during DEAE-Sepharose C1-6B chromatography of monoamine oxidase. Monoamine oxidase was characterized physico-chemically in terms of molecular weight, electrophoretic mobility, iso-electric point, amino acid composition and specific activity. The molecular weight was estimated to be 234.5 K by exclusion chromatography and with iso-electric focusing the pI was estimated to be 5.6.
首次将人血浆过氧化氢酶和单胺氧化酶纯化至均一状态。借助DEAE - 琼脂糖凝胶CL - 6B和琼脂糖凝胶CL - 6B色谱法纯化了3200倍的单胺氧化酶，其不含过氧化氢酶、醛脱氢酶和还原酶活性。在单胺氧化酶的DEAE - 琼脂糖凝胶C1 - 6B色谱过程中获得了均一的过氧化氢酶。从分子量、电泳迁移率、等电点、氨基酸组成和比活性方面对单胺氧化酶进行了物理化学特性鉴定。通过排阻色谱法估计分子量为234.5K，通过等电聚焦估计pI为5.6。
