التفاصيل البيبلوغرافية
| العنوان: |
Integrated landscape of chicken egg chalaza proteomics |
| المؤلفون: |
Jing Pu, Jian Hu, Jing Xiao, Shugang Li, Beibei Wang, Jinqiu Wang, Fang Geng |
| المصدر: |
Poultry Science, Vol 103, Iss 5, Pp 103629- (2024) |
| بيانات النشر: |
Elsevier, 2024. |
| سنة النشر: |
2024 |
| المجموعة: |
LCC:Animal culture |
| مصطلحات موضوعية: |
chicken egg, chalaza, proteome, phosphorylation, N-Glycosylation, Animal culture, SF1-1100 |
| الوصف: |
ABSTRACT: Chicken egg chalaza (CLZ) is a natural colloidal structure in eggs that exists as an egg yolk stabilizer and is similar in composition to egg white. In this study, the proteome, phosphoproteome, and N-glycoproteome of CLZ were characterized in depth. We hydrolyzed the CLZ proteins and enriched the phosphopeptides and glycopeptides. We identified 45 phosphoproteins and 80 N-glycoproteins, containing 59 phosphosites and 203 N-glycosylation sites, respectively. Typically, the ovalbumin in CLZ was both phosphorylated and N-glycosylated, with 4 phosphosites and 4 N-glycosylation sites. Moreover, we identified 2 N-glycosylated subunits of ovomucin, mucin-5B and mucin-6, with 32 and nine N- glycosylation sites, respectively. Analysis of the phosphorylation and N-glycosylation status of CLZ proteins could provide novel insights into the structural and functional characteristics of CLZ. |
| نوع الوثيقة: |
article |
| وصف الملف: |
electronic resource |
| اللغة: |
English |
| تدمد: |
0032-5791 |
| Relation: |
http://www.sciencedirect.com/science/article/pii/S0032579124002086; https://doaj.org/toc/0032-5791 |
| DOI: |
10.1016/j.psj.2024.103629 |
| URL الوصول: |
https://doaj.org/article/5715b84ab4bc4731afb1bd23c2ab2cfa |
| رقم الانضمام: |
edsdoj.5715b84ab4bc4731afb1bd23c2ab2cfa |
| قاعدة البيانات: |
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