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- W1996871710 abstract "The human chorionic gonadotropin beta-subunit tryptic COOH-terminal peptide (residues 123–145) which contains 3 serine-linked sugar chains was isolated. The sugar chains were cleaved by beta-elimination and then separated by gel filtration. The peaks were pooled and their compositions determined. the products of serial glycosidase digestion and periodate oxidation of the intact glycopeptide were also characterized. Of the serine-linked sugar chains, 13% were the hexasaccharide NeuAc alpha2,3 Gal beta1,3 (NeuAc alpha2,3 Gal beta1,4 GlcNAc beta1,6) GalNAc, 34% the tetrasaccharide NeuAc alpha2,3 Gal beta1,3 (NeuAc alpha2,6) GalNAc, 43% the trisaccharide NeuAc alpha2,3 Gal beta1,3 GalNAc and 10% the disaccharide NeuAc alpha2,6 GalNAc." @default.
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- W1996871710 date "1985-01-01" @default.
- W1996871710 modified "2023-10-15" @default.
- W1996871710 title "The structures of the serine-linked sugar chains on human chorionic gonadotropin" @default.
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- W1996871710 doi "https://doi.org/10.1016/0006-291x(85)90610-2" @default.
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