Purification and properties of soluble NADH-cytochrome b5 reductase of rabbit erythrocytes.

@article{Yubisui1982PurificationAP,
  title={Purification and properties of soluble NADH-cytochrome b5 reductase of rabbit erythrocytes.},
  author={Toshitsugu Yubisui and Masaru Takeshita},
  journal={Journal of biochemistry},
  year={1982},
  volume={91 5},
  pages={1467-77}
}
Soluble NADH-cytochrome b5 reductase was purified from rabbit erythrocytes to homogeneity by simple procedures developed in this study including fractionation with ammonium sulfate, gel filtration on a Sephadex G-75 column, and affinity chromatography on a 5'-AMP-Sepharose 4B column. The enzyme was purified about 12,000-fold from hemolysate in terms of NADH-cytochrome b5 reductase activity with a high yield of 40%. The purified enzyme has absorption maxima at 273, 390, and 462 nm, and shoulders… CONTINUE READING