Purification and Characterization of a Phosphoenolpyruvate Phosphatase from Brassica nigra Suspension Cells.

@article{Duff1989PurificationAC,
  title={Purification and Characterization of a Phosphoenolpyruvate Phosphatase from Brassica nigra Suspension Cells.},
  author={Stephen M. G. Duff and Daniel D. Lefebvre and William C Plaxton},
  journal={Plant physiology},
  year={1989},
  volume={90 2},
  pages={734-41}
}
Phosphoenolpyruvate phosphatase from Brassica nigra leaf petiole suspension cells has been purified 1700-fold to apparent homogeneity and a final specific activity of 380 micromole pyruvate produced per minute per milligram protein. Purification steps included: ammonium sulfate fractionation, S-Sepharose, chelating Sepharose, concanavalin A Sepharose, and Superose 12 chromatography. The native protein was monomeric with a molecular mass of 56 kilodaltons as estimated by analytical gel… CONTINUE READING