Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3 alpha-hydroxysteroid dehydrogenase.

@article{Bello1994PurificationON,
  title={Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3 alpha-hydroxysteroid dehydrogenase.},
  author={Barbara Del Bello and Emilia Maellaro and Lidia Sugherini and Annalisa Santucci and Mario Comporti and A Casini},
  journal={The Biochemical journal},
  year={1994},
  volume={304 ( Pt 2)},
  pages={385-90}
}
Rat liver cytosol has been found to reduce dehydroascorbic acid (DHAA) to ascorbic acid in the presence of NADPH. The enzyme responsible for such activity has been purified by ammonium sulphate fractionation, DEAE-Sepharose, Sephadex G-100 SF and Reactive Red column chromatography, with an overall recovery of 27%. SDS/PAGE of the purified enzyme showed one single protein band with an M(r) of 37,500. A similar value (36,800) was found by gel filtration on a Sephadex G-100 SF column. The results… CONTINUE READING
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