Characterization of fucosyl glycopeptides from cell surface and cellular material of rat fibroblasts

Approximately 70% of fucose-labeled glycopeptides from the cell surface and cellular material of rat fibroblasts (3Y1B cells) were hydrolyzed by endo-β-N-acetylglucosaminidase D in the presence of neuraminidase, β-glactosidase and β-N-acetylglucosaminidase. Structure of the suspceptible 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-β-N-acethylglucosaminidase H and α-mannosidase, and appeared to be a mixture of glycopeptides with unique structures.