Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.

@article{Chen1991RecombinantRE,
  title={Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.},
  author={Z. Chen and G. Koelsch and H. Han and X. Wang and X. Lin and J. Hartsuck and J. Tang},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 18},
  pages={
          11718-25
        }
}
  • Z. Chen, G. Koelsch, +4 authors J. Tang
  • Published 1991
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • A cDNA clone, which contained the complete rhizopuspepsin structure and the putative proregion, was placed in three different Escherichia coli expression vectors for the synthesis of rhizopuspepsinogen (Rpg). Recombinant Rpgs which were expressed in the cytosol of E. coli as inclusion bodies (cRpg and tRpg) were not active. After solubilization in 6 M urea and refolding by rapid dilution, both of these Rpgs were purified to homogeneity. The third zymogen, pRpg, which was secreted to the… CONTINUE READING
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