Binding of proteolytically-degraded human colonic mucin glycoproteins to the Gal/GalNAc adherence lectin of Entamoeba histolytica.

@article{Chadee1990BindingOP,
  title={Binding of proteolytically-degraded human colonic mucin glycoproteins to the Gal/GalNAc adherence lectin of Entamoeba histolytica.},
  author={Kris Chadee and Charles M. Ndarathi and Kathy Keller},
  journal={Gut},
  year={1990},
  volume={31 8},
  pages={890-5}
}
Rat and human colonic mucin glycoproteins bind to the Gal/GalNAc adherence lectin on the surface of Entamoeba histolytica in vitro, thus inhibiting the organism from adhering to and lysing the target cells. Human colonic mucin glycoproteins were isolated by Sepharose 4B gel filtration chromatography, they were proteolytically degraded with trypsin, pronase, and papain, and the glycoprotein fractions were reisolated by Sephacryl S-200 gel filtration chromatography. Binding of the mucin… CONTINUE READING

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