Inhibition of trypanosomal cysteine proteinases by their propeptides.

@article{Lalmanach1998InhibitionOT,
  title={Inhibition of trypanosomal cysteine proteinases by their propeptides.},
  author={Gilles Lalmanach and Fabien Lecaille and Jair Ribeiro Chagas and E. M. L. Authi{\'e} and Julio Scharfstein and Maria Aparecida Juliano and Francis L Gauthier},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 39},
  pages={
          25112-6
        }
}
The ability of the prodomains of trypanosomal cysteine proteinases to inhibit their active form was studied using a set of 23 overlapping 15-mer peptides covering the whole prosequence of congopain, the major cysteine proteinase of Trypanosoma congolense. Three consecutive peptides with a common 5-mer sequence YHNGA were competitive inhibitors of congopain. A shorter synthetic peptide consisting of this 5-mer sequence flanked by two Ala residues (AYHNGAA) also inhibited purified congopain. No… CONTINUE READING
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