一种从大鼠肝脏中纯化环氧水解酶的简单方法。
A simple method for purification of epoxide hydratase from rat liver.
作者信息
Knowles R G, Burchell B
出版信息
Biochem J. 1977 May 1;163(2):381-3. doi: 10.1042/bj1630381.
Abstract
Rat liver epoxide hydratase was purified 460-fold to homogeneity by detergent solubilization and ion-exchange chromatography. The enzyme obtained in high yield (36%) exhibited a specific activity of 479nmol of styrene glycol formed/min per mg of protein, with styrene oxide as substrate. Only one polypeptide-staining band, mol.wt. 49500, was visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis.
摘要
通过去污剂增溶和离子交换色谱法，将大鼠肝脏环氧化物水合酶纯化了460倍，达到了均一性。以氧化苯乙烯为底物时，该酶的高产率（36%）表现出每毫克蛋白质每分钟形成479nmol苯乙二醇的比活性。在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳后，仅可见一条分子量为49500的多肽染色带。
Zotero 插件