Purification and crystallization of rhizopuspepsin: the use of nickel chelation chromatography to select for catalytically active species.

@article{Flentke1999PurificationAC,
  title={Purification and crystallization of rhizopuspepsin: the use of nickel chelation chromatography to select for catalytically active species.},
  author={G. R. Flentke and J. Gliński and K. Satyshur and D. Rich},
  journal={Protein expression and purification},
  year={1999},
  volume={16 2},
  pages={
          213-20
        }
}
  • G. R. Flentke, J. Gliński, +1 author D. Rich
  • Published 1999
  • Chemistry, Medicine
  • Protein expression and purification
  • A new method to obtain pure zymogen-derived peptidases is presented. The key strategy is to install a polyhistidine peptide tag on the N-terminus of the propeptide sequence of a zymogen. After expression, purification, and folding of the protein, autocatalytic posttranslational cleavage and filtration through a nickel affinity column gives pure, functional peptidase. This method takes advantage of the nickel affinity chromatography system that removes both zymogen peptide and nonfunctional… CONTINUE READING
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    References

    SHOWING 1-10 OF 28 REFERENCES
    Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.
    • 30
    The amino acid sequence of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis.
    • K. Takahashi
    • Medicine, Biology
    • The Journal of biological chemistry
    • 1987
    • 25
    Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen.
    • 95
    • PDF
    Amino acid sequence of rhizopuspepsin isozyme pI 5.
    • 26
    Intramolecular activation of porcine pepsinogen.
    • 62
    • PDF