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Faculty Publications
Deglycosylation Studies On Tracheal Mucin Glycoproteins
Document Type
Article
Journal/Book/Conference Title
Biochemistry
Volume
26
Issue
17
First Page
5315
Last Page
5322
Abstract
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.
Department
Department of Chemistry
Original Publication Date
1-1-1987
DOI of published version
10.1021/bi00391a015
Recommended Citation
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.
https://scholarworks.uni.edu/facpub/4743