The N terminus of the MUC2 mucin forms trimers that are held together within a trypsin-resistant core fragment.

@article{Godl2002TheNT,
  title={The N terminus of the MUC2 mucin forms trimers that are held together within a trypsin-resistant core fragment.},
  author={Klaus Godl and Malin E. V. Johansson and Martin E. Lidell and Matthias M{\"o}rgelin and Hasse Karlsson and Fredrik J. Olson and James R. Gum and Young Soo Kim and Gunnar C Hansson},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 49},
  pages={47248-56}
}
The N terminus of the human MUC2 mucin (amino acids 1-1397) has been expressed as a recombinant tagged protein in Chinese hamster ovary cells. The intracellular form was found to be an endoglycosidase H-sensitive monomer, whereas the secreted form was an oligomer that gave monomers upon disulfide bond reduction. The secreted MUC2 N terminus contained a trypsin-resistant core fragment. Edman sequencing and mass spectrometry of the peptides obtained localized this core fragment to the C-terminal… CONTINUE READING