1. Purification of thiol:protein-disulfide oxidoreductase from bovine liver.
- Author
-
Bjelland S, Foltmann B, and Wallevik K
- Subjects
- Animals, Cattle, Chromatography, Gel, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Hot Temperature, Protein Denaturation, Liver enzymology, Oxidoreductases isolation & purification, Protein Disulfide Reductase (Glutathione) isolation & purification
- Abstract
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.
- Published
- 1984
- Full Text
- View/download PDF