Deglycosylation studies on tracheal mucin glycoproteins.


Following several model experiments, conditions were developed for optimal deglycosylation of tracheal mucin glycoproteins. Exposure of rigorously dried material to trifluoromethanesulfonic acid at 0 degree C for up to 8 h results in cleavage of essentially all fucose, galactose, and N-acetylglucosamine, about 80% of the N-acetylneuraminic acid (NeuNAc), and a variable amount of N-acetylgalactosamine (GalNAc), the sugar involved in linkage to protein. Residual N-acetylneuraminic acid is sialidase susceptible and apparently in disaccharide units, presumably NeuNAc2----GalNAc. The remaining N-acetylgalactosamine is mostly present as monosaccharides, and a few Gal beta 1----3GalNAc alpha units are also present; both are cleaved by appropriate enzymatic treatment. The saccharide-free proteins obtained from either human or canine mucin glycoproteins have molecular weights of about 100,000 and require chaotropic agents or detergents for effective solubilization.


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@article{Woodward1987DeglycosylationSO, title={Deglycosylation studies on tracheal mucin glycoproteins.}, author={H D Woodward and Nancy J. Ringler and Rajesh Selvakumar and Ira Mitchell Simet and Veer P. Bhavanandan and Eugene A. Davidson}, journal={Biochemistry}, year={1987}, volume={26 17}, pages={5315-22} }