Purification and characterization of a membrane-bound and a secreted mucin-type glycoprotein carrying the carcinoma-associated sialyl-Lea epitope on distinct core proteins.

@article{Baeckstrm1991PurificationAC,
  title={Purification and characterization of a membrane-bound and a secreted mucin-type glycoprotein carrying the carcinoma-associated sialyl-Lea epitope on distinct core proteins.},
  author={Dan Baeckstr{\"o}m and Gunnar C Hansson and Olle Nilsson and Catrine Johansson and Sandra J Gendler and Leif Lindholm},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 32},
  pages={21537-47}
}
Two mucin-type glycoproteins detected by the monoclonal antibody C50, which reacts with the carcinoma-associated sialyl-Lewis a and sialyl-lactotetraose epitopes, were found in secreted and solubilized materials from the colon carcinoma cell line COLO 205. The larger glycoprotein (H-CanAg; heavy cancer antigen) was predominantly found in extracts of cells grown in vitro or as nude mice xenografts whereas the smaller species (L-CanAg; light cancer antigen) was the major component in spent… CONTINUE READING
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