Porcine spleen cathepsin H hydrolyzes oligopeptides solely by aminopeptidase activity.

@article{Takahashi1988PorcineSC,
  title={Porcine spleen cathepsin H hydrolyzes oligopeptides solely by aminopeptidase activity.},
  author={Takayuki Takahashi and A H Dehdarani and Jin Tang},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 22},
  pages={10952-7}
}
Cathepsin H purified from porcine spleens was studied for its specificity against various peptide and denatured protein substrates. The enzyme degraded all peptide substrates exclusively by an aminopeptidase activity. The enzyme preferentially released NH2-terminal amino acid residues with large hydrophobic (Phe, Trp, Leu, and Tyr) or basic (Arg and Lys) side chains. Amino acids containing small or polar side chains were not released. Peptides with a proline in the NH2-terminal or penultimate… CONTINUE READING

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References

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Showing 1-4 of 4 references

Mammalian Proteoses (Barrett

  • J. K. McDonald, A. J. Barrett
  • 1986

Proteinases in Academic Press, London Mammalian Cells and Tissues

  • J. K. McDonald, C. Schwabe
  • (Barrett, A. J.,
  • 1977

Proteinuses in Mammalian Cells and Tissues

  • A. J. Barrett
  • (Barrett, A. J.,
  • 1977

Cathepsin H Hydrolyzes Oligopeptides by Aminopeptidase Activity 10955

  • E. D. Wachsmuth, I. Fritze, G. Pfleiderer
  • CH Fbpain A B C D L5K3lK21K1LK- t CH Pbpain " A B…
  • 1966

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