Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.

@article{Hernndez2000SquashTI,
  title={Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.},
  author={J. L. Figueroa Hern{\'a}ndez and J M Gagnon and Laurent Chiche and Thi M.-D. Nguyen and J P Andrieu and Annie Heitz and T Trinh Hong and T T Pham and Dung Le Nguyen},
  journal={Biochemistry},
  year={2000},
  volume={39 19},
  pages={5722-30}
}
Three trypsin inhibitors (TIs), from the seeds of the squash Momordica cochinchinensis (MCo), have been isolated and purified using gel filtration, ion exchange chromatography, and reverse-phase HPLC. Their sequences could be determined only after proteolytic cleavages. In the case of MCoTI-I and -II, it was shown that their polypeptide backbones are cyclic, a structure that has never been described in squash TIs. They contain 34 amino acid residues with 3 disulfide bridges and measured… CONTINUE READING
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