One step affinity recovery of 3α-hydroxysteroid dehydrogenase from cloned Escherichia coli.

@article{Yang2015OneSA,
  title={One step affinity recovery of 3α-hydroxysteroid dehydrogenase from cloned Escherichia coli.},
  author={Hailin Yang and Yanan Fang and Zhizhen Wang and L. X. Zhang},
  journal={Journal of chromatography. B, Analytical technologies in the biomedical and life sciences},
  year={2015},
  volume={991},
  pages={
          79-84
        }
}
3α-Hydroxysteroid dehydrogenase (3α-HSD), from Comamonas Testosterone, catalyze reversibly the oxidoreduction of 3α-hydroxyl groups of the steroid hormones. The gene encoding 3α-HSD (hsdA) from Comamonas Testosterone was expressed in Escherchia coli BL21 (DE3). A protocol for recovering 3α-HSD based on affinity strategy was designed and employed. Deoxycholic acid was chosen as the affinity ligand, and it was linked to Sepharose 4B with the aid of the spacers as cyanuric chloride and… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 13 REFERENCES

Affinity purification of serine proteinase from Deinagkistrodon acutus venom.

  • Journal of chromatography. B, Analytical technologies in the biomedical and life sciences
  • 2007

3 a - Hydroxysteroid dehydrogenase / carbonyl reductase from Comamonas testosteroni : biological significance , three - dimensional structure and gene regulation

G. Xiong Maser, C. Grimm, R. Ficner, K. Reuter
  • Chem . Biol . Interact .
  • 2001