Identification of the Duck Egg White N-Glycoproteome and Insight into the Course of Biological Evolution
| Autor: | Russell Keast, Yinqiang Huo, Fang Geng, Yaqi Meng, Ning Qiu, Haohao Sun |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Proteomics
0106 biological sciences Protein glycosylation Glycosylation animal structures Biology 01 natural sciences Egg White Riboflavin-binding protein Animals Glycoproteins Egg Proteins 010401 analytical chemistry General Chemistry Biological evolution Biological Evolution 0104 chemical sciences Ducks Biochemistry Posttranslational modification Identification (biology) General Agricultural and Biological Sciences Chickens human activities 010606 plant biology & botany Egg white |
| Zdroj: | Journal of Agricultural and Food Chemistry. 67:9950-9957 |
| ISSN: | 1520-5118 0021-8561 |
| DOI: | 10.1021/acs.jafc.9b03059 |
| Popis: | Protein glycosylation is a ubiquitous posttranslational modification that modulates protein properties, thereby influencing bioactivities within a system. Duck egg white (DEW) proteins exhibit diverse biological properties compared with their chicken egg white (CEW) counterparts, which might be related to glycosylation. N-Glycoproteome analysis of DEW was conducted, and a total of 231 N-glycosites from 68 N-glycoproteins were identified. Gene ontology analysis was used to elucidate the biofunctions of DEW N-glycoproteins and compare them with those of CEW, which showed that the differences mostly involved molecular functions and biological processes. The biological functions of DEW N-glycoproteins were illuminated through bioinformatics analysis and comparison with CEW orthologues, which showed different allergenicities and antibacterial abilities. These divergences might be initiated by specific alterations in glycosylation, which can enhance the proteolysis resistance and protein steric hindrance. These results provide new insights for discovering the effects of N-glycosylation on biofunctions during the divergence of homologous proteins. |
| Databáze: | OpenAIRE |
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