大鼠肝脏单胺氧化酶电泳可分离的多种形式的性质
The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase.
作者信息
Houslay M D, Tipton K F
出版信息
Biochem J. 1973 Sep;135(1):173-86. doi: 10.1042/bj1350173.
Abstract
- Treatment of a partly purified preparation of rat liver monoamine oxidase with the chaotropic agent sodium perchlorate caused the enzyme to migrate as a single band of activity of polyacrylamide-gel electrophoresis, whereas the untreated enzyme separated into a number of bands. 2. Treatment with the chaotropic agent caused no loss of enzyme activity towards benzylamine, dopamine or tyramine. 3. The activities of the untreated preparation towards different substrates were inhibited to different extents by heat treatment and by some inhibitors. No such differences could be detected after the enzyme preparation had been treated with sodium perchlorate. 4. Lipid material, which could be separated by gel filtration, was liberated from the enzyme preparation by sodium perchlorate treatment. 5. The molecular weight of the treated enzyme was found to be 380000+/-38000. 6. Perchlorate treatment altered the solubility of the enzyme. 7. A continuous assay method for monoamine oxidase is described.
摘要
- 用离液剂高氯酸钠处理大鼠肝脏单胺氧化酶的部分纯化制剂，使得该酶在聚丙烯酰胺凝胶电泳中作为单一活性条带迁移，而未处理的酶则分离成多条条带。2. 用离液剂处理不会导致该酶对苄胺、多巴胺或酪胺的活性丧失。3. 未处理制剂对不同底物的活性受到热处理和某些抑制剂的不同程度抑制。在用高氯酸钠处理酶制剂后未检测到此类差异。4. 可通过凝胶过滤分离的脂质物质通过高氯酸钠处理从酶制剂中释放出来。5. 发现处理后酶的分子量为380000±38000。6. 高氯酸盐处理改变了酶的溶解度。7. 描述了一种单胺氧化酶的连续测定方法。
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