NADPH-cytochrome c (P-450) reductase from liver microsomes of phenobarbital-treated rats has been purified in a single step by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, enzyme assay, and radioimm
Purification of glutathione reductase from gerbil liver in two steps
β Scribed by Nguyen Le Trang; Kuldeep K. Bhargava; Anthony Cerami
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 771 KB
- Volume
- 133
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
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 of the purified enzyme are reported.
π SIMILAR VOLUMES
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
Glucose isomerase (EC 5.3.1.5) catalyzes the quantitative isomerisation of 5-azido-5-deoxy-n-gluco-(7) and -L-idofuranose (9), respectively, into the corresponding ketoses, 5-azido-5-deoxy-n-fructopyranose (8) and -L-sorbopyranose (lo), respectively. Upon catalytic hydrogenation over palladium-oncha