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- W2022225024 abstract "Abstract Glycopeptides located at asparagine residues at position 52 in the α-subunit and at position 7 in the β-subunit of human follicle-stimulating hormone (FSH) were obtained by pronase digestion of the intact human FSH molecule. The glycopeptide fractions were isolated by gel filtration and by high-voltage electrophoresis on paper at pH 6 and/or pH 3.5. Alkaline degradation studies performed on the α- and β-subunits of human follicle-stimulating hormone confirmed that carbohydrate moieties linked O -glycosidically to threonine or to serine are not present in either subunit. Carbohydrate composition of both α-52 and β-7 glycopeptides was similar. Sialic acid, mannose, galactose, N -acetylglucosamine, N -acetylgalactosamine and fucose were present in a ratio of 3:4:3:4:1:1 in both glycopeptides. The results of sequential enzymatic digestion revealed that the peripheral monosaccharide sequence of both the α-52 and β-7 glycopeptides consisted of three chains each containing the following sequence: sialic acid galactose β - N -acetylglucosamine mannose. The composition of the undigested ‘inner core’ of both carbohydrate moieties was found to be similar and consisted of one residue/mol glycopeptide each of mannose, N -acetylglucosamine, N -acetylgalactosamine, and fucose. The unique presence of GalNAc attached to an N -glycosidically linked GlcNAc was confirmed by hexosamine analysis on an amino acid analyzer, by thin-layer chromatography, by digestion with enzymes such as exo- α - N -acetylgalactosaminidase and endoglycosidases D and H, and by ion-exchange chromatography on DEAE-Sephacel. The monosaccharide sequence of the α-52 and the β-7 glycopeptides of human follicle-stimulating hormone is shown below and is identical to the one at the α-78 position." @default.
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- W2022225024 date "1982-10-01" @default.
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- W2022225024 title "Studies on the unique presence of an N-acetylgalactosamine residue in the carbohydrate moieties of human follicle-stimulating hormone" @default.
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- W2022225024 doi "https://doi.org/10.1016/0304-4165(82)90299-9" @default.
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