作者: Daniel Ambort , Sjoerd van der Post , Malin E. V. Johansson , Jenny MacKenzie , Elisabeth Thomsson
DOI: 10.1042/BJ20102066
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摘要: The colonic human MUC2 mucin forms a polymeric gel by covalent disulfide bonds in its N- and C-termini. middle part of is largely composed two highly O-glycosylated domains that are interrupted CysD domain unknown function. We studied function as recombinant proteins fused to removable immunoglobulin Fc domain. Analysis affinity-purified fusion native electrophoresis filtration showed they formed oligomeric complexes. the individual isolated parts dimers both when flanked tandem repeats without these. Cleavages non-reduced analysis MS revealed localization all five predicted C-mannosylated site was not glycosylated. All were within peptides showing stabilized intramolecular non-covalent nature. These observations suggest act cross-links gel, thereby determining pore sizes mucus.