Isolation of two novel sialyl-Lewis X-active oligosaccharides by high-performance liquid affinity chromatography using monoclonal antibody Onc-M26
| Autor: | Bo Nilsson, Brown Joseph P, WeiTong Wang, David Zopf, Torgny Lundgren, Frank Lindh, Gunnar Grönberg, Holly Mentzer-Dibert |
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| Rok vydání: | 1992 |
| Předmět: |
Magnetic Resonance Spectroscopy
medicine.drug_class Molecular Sequence Data Biophysics Lewis X Antigen Oligosaccharides Monoclonal antibody Biochemistry Epitope chemistry.chemical_compound Affinity chromatography Antigen medicine Carbohydrate Conformation Tetrasaccharide Humans Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification biology Milk Human Antibodies Monoclonal Oligosaccharide Sialyl-Lewis X chemistry Carbohydrate Sequence biology.protein Thermodynamics Female Antibody |
| Zdroj: | Archives of biochemistry and biophysics. 292(2) |
| ISSN: | 0003-9861 |
| Popis: | A monoclonal antibody, Onc-M26, that recognizes a cancer-associated antigen expressed by most human adenocarcinomas of the breast was shown previously to recognize a carbohydrate epitope carried on a hexaglycosyl ganglioside carrying the sialyl-Lewis X (SLe x ) antigen (P. S. Linsley et al. , 1988, Cancer Res. 48, 2138–2148). Evidence that the antibody binds even more avidly to minor gangliosides containing more complex carbohydrate chains prompted us to search for a higher affinity epitope among sialylated oligosaccharides from pooled human milk. Affinity chromatography of a partially purified fraction of monosialylated milk oligosaccharides on a column containing monoclonal antibody Onc-M26 bound to a macroporous silica matrix gave a peak with a retention volume significantly greater than that of a standard SLe x -active hexasaccharide. The retained material consisted of two nonasaccharides, each containing the SLe x tetrasaccharide sequence, Neu5Acα2–3Galβ1–4(Fucα1–3)GlcNAc, linked β1–6 to a 3,6-disubstituted galactosyl residue. |
| Databáze: | OpenAIRE |
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