Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat.
Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat fibroblasts (3Y1B cells) were hydrolyzed by endo-beta-N-acetylglucosaminidase D in the presence of neuraminidase, beta-galactosidase and beta-N-acetylglucosaminidase. Structure of the susceptible glycopeptides were found to be very similar to non-membrane glycopeptides of the complex heteropolysaccharide unit, such as the sialylated glycopeptides of thyroglobulin. On the other hand, the resistant glycopeptides were also refractory toward endo-beta-N-acetylglucosaminidase H and alpha-mannosidase, and appeared to be a mixture of glycopeptides with unique structures.
D000118:Acetylglucosaminidase; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism*; D005643:Fucose / Q000378:metabolism*; D005696:Galactosidases; D005947:Glucose / Q000378:metabolism; D006020:Glycopeptides / Q000032:analysis / Q000378:metabolism*; D008361:Mannosidases; D008970:Molecular Weight; D009439:Neuraminidase; D051381:Rats; D012794:Sialic Acids / Q000032:analysis
D006020:Glycopeptides; D012794:Sialic Acids; D005643:Fucose; D005696:Galactosidases; D008361:Mannosidases; D009439:Neuraminidase; D000118:Acetylglucosaminidase; D005947:Glucose