Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme.

@article{Copeland1995RecombinantHD,
  title={Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme.},
  author={Robert A Copeland and John Paul Davis and Randine L. Dowling and Dominique Lombardo and KevinR. Murphy and Terrell Ann Patterson},
  journal={Archives of biochemistry and biophysics},
  year={1995},
  volume={323 1},
  pages={
          79-86
        }
}
An N-terminally truncated cDNA for human dihydroorotate dehydrogenase (DHODase) was placed under the control of the inducible T7 lac promoter in a pyrimidine auxotrophic strain of Escherichia coli lacking the endogenous enzyme. Induction of gene expression rescued growth in media lacking exogenous pyrimidines. The recombinant enzyme was purified to homogeneity from detergent extracts of bacterial membranes by two chromatographic steps. The purity of the resulting enzyme was judged to be > 95… CONTINUE READING
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