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

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