从牛肝脏中纯化硫醇：蛋白质二硫键氧化还原酶。
Purification of thiol:protein-disulfide oxidoreductase from bovine liver.
作者信息
Bjelland S, Foltmann B, Wallevik K
出版信息
Anal Biochem. 1984 Nov 1;142(2):463-6. doi: 10.1016/0003-2697(84)90490-1.
A rapid purification procedure of thiol:protein-disulfide oxidoreductase (EC 1.8.4.2) from bovine liver has been developed. The procedure is based on that of D. F. Carmichael, J. E. Morin, and J. E. Dixon (1977, J. Biol. Chem. 252, 7163-7167), and contains the following steps: homogenization in Triton X-100, selective heat denaturation, chromatography on CM-Sephadex C-50, and chromatography on DEAE-Sephadex A-50. The final preparation has a high specific activity and a high level of purity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
已开发出一种从牛肝中快速纯化硫醇
蛋白质二硫键氧化还原酶（EC 1.8.4.2）的方法。该方法基于D. F. 卡迈克尔、J. E. 莫林和J. E. 迪克森（1977年，《生物化学杂志》252卷，7163 - 7167页）的方法，包含以下步骤：在Triton X - 100中匀浆、选择性热变性、在CM - Sephadex C - 50上进行色谱分离以及在DEAE - Sephadex A - 50上进行色谱分离。通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳判断，最终制品具有高比活性和高纯度。
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