哺乳动物D-2-羟基酸脱氢酶的测定、纯化及性质
Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase.
作者信息
Cammack R
出版信息
Biochem J. 1969 Oct;115(1):55-64. doi: 10.1042/bj1150055.
Abstract
- A new method is described for the measurement of d-2-hydroxy acid dehydrogenase in samples of animal tissues. 2. The distribution of the enzyme in a number of animals was determined. Of the animal tissues tested, the most active source of the enzyme was found to be rabbit kidney cortex. 3. The enzyme was purified from rabbit kidney to a stage at which it appears to be homogeneous in the analytical ultracentrifuge and on polyacrylamide-gel electrophoresis. 4. The molecular weight was estimated by gel filtration to be approx. 102000; combination of gelfiltration data and the sedimentation coefficient gave a value of 95000. 5. The purified enzyme has a spectrum typical of a flavoprotein. The change induced in the spectrum on addition of d-malate or d-lactate suggests the formation of a flavin semiquinone. 6. Flavin can be removed by treatment with acid ammonium sulphate, and activity can be restored to the inactive apoenzyme by addition of FAD, but not of FMN or riboflavin. 7. Studies of acceptor specificity showed that the enzyme has a relatively weak d-2-hydroxy acid oxidase activity.
摘要
- 本文描述了一种测定动物组织样品中d-2-羟基酸脱氢酶的新方法。2. 测定了该酶在多种动物中的分布。在所测试的动物组织中，发现该酶最活跃的来源是兔肾皮质。3. 从兔肾中纯化该酶，直至在分析超速离心机和聚丙烯酰胺凝胶电泳中呈现均一状态。4. 通过凝胶过滤法估计分子量约为102000；结合凝胶过滤数据和沉降系数得出的值为95000。5. 纯化后的酶具有黄素蛋白的典型光谱。加入d-苹果酸或d-乳酸后光谱的变化表明形成了黄素半醌。6. 用酸性硫酸铵处理可去除黄素，通过添加FAD可使无活性的脱辅基酶恢复活性，但添加FMN或核黄素则不能。7. 受体特异性研究表明，该酶具有相对较弱的d-2-羟基酸氧化酶活性。
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