The asparagine-linked sugar chains of human follicle-stimulating hormone.
The asparagine-linked sugar chains of human follicle-stimulating hormone (hFSH) were liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and NaB3H4 reduction. Ninety-five percent of the oligosaccharides were acidic and all were converted to a mixture of neutral oligosaccharides on sialidase treatment. The mixture of neutral oligosaccharides was subjected to sequential immobilized lectin column chromatography on E-PHA-agarose, AAL-Sepharose, and Con A-Sepharose, and six fractions were obtained. The results of sequential exoglycosidase digestion of each oligosaccharide and methylation analysis led us to propose that the asparagine-linked sugar chains of hFSH are a mixture of complex-type bi-, tri-, and tetraantennary sialylated sugar chains with and without a fucose residue linked at the C-6 position of the proximal N-acetylglucosamine. Some of these sugar chains contain bisecting N-acetylglucosamine residue.
D000107:Acetylation; D001216:Asparagine; D001894:Borohydrides; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005640:Follicle Stimulating Hormone; D006801:Humans; D009844:Oligosaccharides / Q000032:analysis*
D001894:Borohydrides; D009844:Oligosaccharides; D001216:Asparagine; D005640:Follicle Stimulating Hormone