Primary structure of the major glycan from human seminal transferrin |
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Authors: | Gabriele D'Andrea Anna M D'Alessandro M Luisa Salucci and Arduino Oratore |
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Institution: | (1) Department of Sciences and Biomedical Technologies and Biometrics, University of L'Aquila, I-67100 L'Aquila, Italy |
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Abstract: | Human seminal transferrin (HSmT) is an iron-containing glycoprotein whose structural properties have not been adequately investigated. The carbohydrate content of the purified glycoprotein amount to 6.1%, and monosaccharide analysis revealed the major oligosaccharide moiety to be of the N-glycoside type. The carbohydrate chains were released from the iron-free form by digestion with peptide N-glycosidase F (PNGase F) in the presence of detergents such as SDS and -octylglucoside. After ethanol precipitation and fractionation on Bio-Gel P-6 and Bio-Gel P-2, the oligosaccharide was further purified on Mono-Q and desalted on Bio-Gel P-2. By 600-MHz1H-NMR spectroscopy, the primary structure of the major N-linked oligosaccharide component was established to be:
Abbreviations used HSmT
human seminal transferrin
- HSrT
human serum transferrin
- PNGase F
peptide-N4-(N-acetyl- -glucosaminyl)asparagine amidase-F (E.C. 3.5.1.52), commonly known as peptide N-glycosidase F
- SDS-PAGE
sodium dodecyl sulphate-polyacrylamide gel electrophoresis
- GLC
gas-liquid chromatography
- FPLC
fast liquid protein chromatography
- EDTA
ethylenediaminetetraacetic acid, disodium salt
- PMFS
phenylmethylsulfonyl fluoride
- GlcNAc
N-acetylglucosamine
- NeuAc
N-acetylneuraminic acid
- Man, Gal
galactose
- Fuc
fucose |
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Keywords: | Human seminal transferrin glycan 1H-NMR spectroscopy |
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