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Comparative Quantitative Phosphoproteomic Analysis of the Chicken Egg during Incubation Based on Tandem Mass Tag Labeling.

Haohao SunNing QiuRussell KeastHong WangBin LiQun HuangShugang Li
Published in: Journal of agricultural and food chemistry (2019)
Protein phosphorylation plays an important role in protein structure and function. To investigate the role of egg protein phosphorylation in chicken embryonic development, a comparative and quantitative phosphoproteomic analysis of fertilized chicken egg white and yolk was performed during incubation. Overall, 215 phosphosites mapped onto 205 phosphopeptides corresponding to 100 phosphoproteins were identified. Among these phosphoproteins, 123 phosphosites from 62 egg proteins were found significantly changed (p < 0.05) at day 12 during incubation. Furthermore, GO analysis suggested that these differentially phosphorylated proteins were associated with various molecular functions, primarily including binding, molecular function regulator, and transport activity. Such findings in this study improved our understanding of the protein molecular functions involved in chicken embryonic development from a protein phosphorylation perspective.
Keyphrases
  • protein protein
  • binding protein
  • small molecule
  • protein kinase
  • single molecule
  • mass spectrometry