蛋白质组
糖基化
蛋白质组学
磷酸化
生物化学
蛋白质磷酸化
定量蛋白质组学
糖蛋白
细胞生物学
生物
化学
磷酸蛋白质组学
基因
蛋白激酶A
作者
Ran Yang,Fang Geng,Xiang Huang,Ning Qiu,Shugang Li,Hui Teng,Lei Chen,Hongbo Song,Qun Huang
出处
期刊:Food Chemistry
[Elsevier]
日期:2020-11-01
卷期号:330: 127167-127167
被引量:29
标识
DOI:10.1016/j.foodchem.2020.127167
摘要
Eggshell matrix (EM) proteins play an important biological role in eggshell mineralization and embryo development. Many studies have demonstrated that some matrix proteins undergo posttranslational modifications, including phosphorylation and glycosylation, which have important regulatory effects on the functional properties of the proteins. Systematic analysis of the proteome, the phosphorylated modified proteome and the glycosylated modified proteome of the chicken EM was performed using a proteomics strategy. A total of 112 phosphorylation sites from 69 phosphoproteins and 297 N-glycosylation sites from 182 N-glycoproteins were identified in the chicken EM. Among all these identified modified proteins, 129 were not identified in the proteome (547 proteins). Therefore, a total of 676 EM proteins were identified in this study. Gene ontology (GO) enrichment analysis indicated that EM proteins and phosphoproteins were mainly enriched in regulation of enzyme activity, while EM N-glycoproteins were enriched in immune response regulation.
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