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Comparative Quantitative Phosphoproteomic Analysis of the Chicken Egg during Incubation Based on Tandem Mass Tag Labeling
journal contribution
posted on 2019-12-04, 00:00 authored by H Sun, N Qiu, Russell KeastRussell Keast, H Wang, B Li, Q Huang, S LiCopyright © 2019 American Chemical Society. 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.
History
Journal
Journal of Agricultural and Food ChemistryVolume
67Issue
48Pagination
13353 - 13361Publisher
ACS PublicationsLocation
Washington, D.C.Publisher DOI
ISSN
0021-8561eISSN
1520-5118Language
engPublication classification
C1 Refereed article in a scholarly journalUsage metrics
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No categories selectedKeywords
chicken eggprotein phosphorylationtandem mass tagquantitative phosphoproteomicschicken embryonic developmentScience & TechnologyLife Sciences & BiomedicinePhysical SciencesAgriculture, MultidisciplinaryChemistry, AppliedFood Science & TechnologyAgricultureChemistryRIBOFLAVIN-BINDING PROTEINCOMPARATIVE PROTEOMIC ANALYSISEGGSHELL MATRIX PROTEINWHITE PROTEINSYOLK PLASMAFUNCTIONAL-PROPERTIESEMBRYONIC-DEVELOPMENTPHOSPHORYLATIONIMPROVEMENTOVALBUMIN
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