alexa Structures of asparagine linked oligosaccharides of immunoglobulins (IgY) isolated from egg-yolk of Japanese quail.
Bioinformatics & Systems Biology

Bioinformatics & Systems Biology

Journal of Glycomics & Lipidomics

Author(s): Matsuura F, Ohta M, Murakami K, Matsuki Y

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Abstract Structures of the Asn linked oligosaccharides of quail egg-yolk immunoglobulin (IgY) were determined in this study. Asn linked oligosaccharides were cleaved from IgY by hydrazinolysis and labelled with p-aminobenzoic acid ethyl ester (ABEE) after N-acetylation. The ABEE labelled oligosaccharides were then fractionated by a combination of Concanavalin A-agarose column chromatography and anion exchange, normal phase and reversed phase HPLC before their structures were determined by sequential exoglycosidase digestion, methylation analysis, HPLC, and 500 MHz 1H-NMR spectroscopy. Quail IgY contained only neutral oligosaccharides of the following categories: the glucosylated oligomannose type (0.6\% Glc alpha 1-3Glc alpha 1-3Man9GlcNAc2; 35.6\%, Glc alpha 1-3Man7-9GlcNAc2). oligomannose type (15.0\%, with the structure Man5-9GlcNAc2) and biantennary complex type with core structures of -Man alpha 1-3(-Man alpha 1-6)Man beta 1-4GlcNAc beta 1-4GlcNAc (9.9\%), -Man alpha 1-3 (GlcNAc beta 1-4)(-Man alpha 1-6)Man beta 1-4GlcNAc beta 1-4GlcNAc (25.1\%) and -Man alpha 1-3(GlcNAc beta 1-4)(-Man alpha 1-6)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc (11.4\%). Although never found in mammalian proteins, glucosylated oligosaccharides (Glc1Man7-9GlcNAc2) have been located previously in hen IgY.
This article was published in Glycoconj J and referenced in Journal of Glycomics & Lipidomics

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