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 °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 Galβ1 → 3GalNAca 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 100000 and require chaotropic agents or detergents for effective solubilization. © 1987, American Chemical Society. All rights reserved.
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Woodward, Harold D.; Davidson, Eugene A.; Simet, Ira M.; Ringler, Nancy J.; Selvakumar, R.; and Bhavanandan, V. P., "Deglycosylation Studies on Tracheal Mucin Glycoproteins" (1987). Faculty Publications. 4743.