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.
Woodward
H D
HD
Department of Biological Chemistry, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.
Ringler
N J
NJ
Selvakumar
R
R
Simet
I M
IM
Bhavanandan
V P
VP
Davidson
E A
EA
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001894:Borohydrides; D001980:Bronchi; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D004285:Dogs; D006026:Glycoside Hydrolases; D006801:Humans; D008970:Molecular Weight; D009077:Mucins / Q000302:isolation & purification; D014132:Trachea
D000596:Amino Acids; D001894:Borohydrides; D002241:Carbohydrates; D009077:Mucins; D006026:Glycoside Hydrolases