Purification and characterization of equine testicular cytochrome P-450 aromatase: comparison with the human enzyme.

@article{Moslemi1997PurificationAC,
  title={Purification and characterization of equine testicular cytochrome P-450 aromatase: comparison with the human enzyme.},
  author={Safa Moslemi and A Vibet and Vassilios Papadopoulos and Laurence Camoin and P Silberzahn and Jean Luc Gaillard},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={1997},
  volume={118 1},
  pages={217-27}
}
Cytochrome P-450 aromatase was purified by five chromatographic steps from adult stallion testis. It was first separated from NADPH-cytochrome P-450 reductase (reductase) on omega-aminohexyl-Sepharose 4B then purified to homogeneity on concanavalin A-Sepharose 4B, hydroxyapatite-Sepharose 4B, DEAE-Sepharose CL-6B and on a second hydroxyapatite-Sepharose 4B… CONTINUE READING