Structure of the N-asparagine-linked oligosaccharide units of human placental beta-glucocerebrosidase.
The N-asparagine-linked oligosaccharide chains of homogeneous human placental beta-glucocerebrosidase were released by hydrazinolysis, and their structures were analyzed. The sequence of sugars, linkage, and anomeric configuration of the glycosidic bonds were determined. Approximately 20% of the released sugar chain was of the typical high mannose type. The balance was of complex type with biantennary and triantennary structures. As a major component, the following trisialylated oligosaccharide was detected: (formula; see text).
D001216:Asparagine / Q000032:analysis*; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005260:Female; D005959:Glucosidases / Q000302:isolation & purification*; D005962:Glucosylceramidase / Q000302:isolation & purification*; D006801:Humans; D008745:Methylation; D009844:Oligosaccharides / Q000032:analysis*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D009844:Oligosaccharides; D001216:Asparagine; D005959:Glucosidases; D005962:Glucosylceramidase