Effect of a supernatant protein on microsomal squalene epoxidase and 2,3-oxidosqualene-lanosterol cyclase.

@article{Saat1976EffectOA,
  title={Effect of a supernatant protein on microsomal squalene epoxidase and 2,3-oxidosqualene-lanosterol cyclase.},
  author={Yeheskel A. Saat and Konrad E Bloch},
  journal={The Journal of biological chemistry},
  year={1976},
  volume={251 17},
  pages={5155-60}
}
Squalene epoxidation catalyzed by rat liver microsomes requires oxygen NADPH, and the 105,000 x g supernatant (S105). The supernatant can be replaced by a partially purified S105 protein (SPF) and phospholipids (Tai, H., and Bloch, K. (1972) J. Biol. Chem. 247, 3767). When washed microsomes are preincubated anaerobically with [14C]squalene and S105 without NADPH, followed by centrifugation and washing to remove the unbound squalene and S105, epoxidation in the presence of O2 and NADPH occurs… CONTINUE READING

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