Glycoblotting of Egg White Reveals Diverse N-Glycan Expression in Quail Species
Autor: | Hiroshi Hinou, Jurgen T. Sanes, Yuan C. Lee, Shin-Ichiro Nishimura |
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Rok vydání: | 2018 |
Předmět: |
0106 biological sciences
Glycan animal structures Glycosylation Blotting Western 01 natural sciences Quail chemistry.chemical_compound Egg White Polysaccharides biology.animal Animals Mountain quail Glycoproteins chemistry.chemical_classification Galliformes biology 010401 analytical chemistry Egg Proteins General Chemistry biology.organism_classification 0104 chemical sciences carbohydrates (lipids) chemistry Biochemistry embryonic structures biology.protein High mannose General Agricultural and Biological Sciences Glycoprotein 010606 plant biology & botany Egg white |
Zdroj: | Journal of agricultural and food chemistry. 67(1) |
ISSN: | 1520-5118 |
Popis: | The glycan part of glycoproteins is known to be involved in the structure and modulatory functions of glycoproteins, serving as ligands for cell-to-cell interactions, and as specific ligands for cell-to-microbe interactions. It is believed that intraspecies and interspecies variations in glycosylation exist. As an approach to better understand glycan diversity, egg whites (EW) from four different quail species are studied by the well-established glycoblotting procedure, a glycan enrichment and analysis method. N-Glycans were classified and the profiles were established for quail egg white samples which showed 21 relevant glycan peaks; 18 peaks were expressed significantly, and 10 glycan peaks are found to be abundant in certain species. The result establishes glycan profiles for Blue Scaled, Bobwhite, Japanese, and Mountain Quail egg whites and shows a unique difference among glycan expressions, particularly, high mannose in Japanese Quail and tetra-antennary glycan structure for other quail species. |
Databáze: | OpenAIRE |
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