The isolated MUC5AC gene product from human ocular mucin displays intramolecular conformational heterogeneity.

@article{Round2007TheIM,
  title={The isolated MUC5AC gene product from human ocular mucin displays intramolecular conformational heterogeneity.},
  author={Andrew N. Round and Terence J. McMaster and Mervyn J. Miles and Anthony P Corfield and Monica Berry},
  journal={Glycobiology},
  year={2007},
  volume={17 6},
  pages={578-85}
}
Atomic force microscopy (AFM) has been used to show that human ocular mucins contain at least three distinct polymer conformations, separable by isopycnic density gradient centrifugation. In this work we have used affinity purification against the anti(mucin peptide core) monoclonal antibody 45M1 to isolate MUC5AC gene products, a major component of human ocular mucins. AFM images confirm that the affinity-purified polymers adopt distinct conformations that coidentify with two of those observed… CONTINUE READING