Enzymatic characterization of purified recombinant human renin.

@article{Pilote1995EnzymaticCO,
  title={Enzymatic characterization of purified recombinant human renin.},
  author={Louise Pilote and Ginette McKercher and Diane Thibeault and Daniel Lamarre},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={1995},
  volume={73 3-4},
  pages={163-70}
}
Renin is a highly specific aspartyl protease of the renin-angiotensin system initially synthesized as preprorenin. Recombinant human prorenin was produced in cell factories from stably transfected DAMP cells, a dog epithelial cell line. The equivalent of 10-15 mg of recombinant human renin was secreted in the supernatant from each cell factory. Following a single affinity chromatography step using a renin inhibitor as the ligand, a 181-fold purification was achieved with 81% recovery of the… CONTINUE READING