Purification of oestrogen synthetase by high-performance liquid chromatography. Two membrane-bound enzymes from the human placenta.

@article{Muto1985PurificationOO,
  title={Purification of oestrogen synthetase by high-performance liquid chromatography. Two membrane-bound enzymes from the human placenta.},
  author={Naoki Muto and Liat Tan},
  journal={Journal of chromatography},
  year={1985},
  volume={326},
  pages={
          137-46
        }
}
Human placental NADPH-cytochrome P-450 reductase, obtained by 2',5'-ADP-Sepharose affinity chromatography, was separated into two reductase-active peaks on a Pharmacia Mono-Q column. By this short, two-step chromatographic procedure, the two reductases were obtained in a homogeneous state with high retention of activity and in over 900-fold purification. Aromatase-reconstituting activity was present only in the higher-molecular-weight reductase (79 000 D), not in the smaller, 70 000 D reductase… CONTINUE READING
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