Horse-liver glutathione reductase: Purification and characterization
✍ Scribed by Concepción Garcìa-Alfonso; Emilia Martìnez-Galisteo; Antonio Llobell; J.Antonio Bárcena; Juan lÓpez-Barea
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 856 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0020-711X
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A new method for the isolation of glutathione reductase which successively utilizes chromatography on 2',5'-ADP-Sepharose 4B and DEAE-Sepharose CL 6B, is described. With these two steps, it was possible to purify to homogeneity the glutathione reductase from gerbil liver. Some molecular properties o
Glutathione reductase has been purified to at least 98% homogeneity from calf liver. An essential part in the procedure involves affinity chromatography on 2',5'-ADP-Sepharose 4B to which the enzyme remains bound in the presence of 0.4 M phosphate. This step separates glutathione reductase from the