Primary structure of the major glycan from human seminal transferrin
| Autor: | Gabriele D'Andrea, Anna Maria D'Alessandro, Arduino Oratore, M L Salucci |
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| Rok vydání: | 1994 |
| Předmět: |
Male
PNGase F Glycan Magnetic Resonance Spectroscopy Detergents Molecular Sequence Data Oligosaccharides Peptide Biochemistry Amidohydrolases Polysaccharides Semen Carbohydrate Conformation Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Monosaccharide chemistry.chemical_classification Chromatography biology Transferrin Protein primary structure Oligosaccharide Carbohydrate Sequence chemistry biology.protein Glycoprotein Hydrogen |
| Zdroj: | Journal of Protein Chemistry. 13:31-36 |
| ISSN: | 1573-4943 0277-8033 |
| DOI: | 10.1007/bf01891990 |
| Popis: | 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 beta-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-MHz 1H-NMR spectroscopy, the primary structure of the major N-linked oligosaccharide component was established to be: [formula: see text] |
| Databáze: | OpenAIRE |
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