Integrated Proteomic and N-Glycoproteomic Analyses of Chicken Egg during Embryonic Development

Abstract

To better appreciate the alterations of egg proteins and their modifications during embryonic development, a comparative and quantitative study was performed aimed at chicken egg white and yolk proteome and <i>N</i>-glycoproteome after 12 days of incubation using tandem mass tag (TMT)-labeling technology in conjunction with reversed-phase high-performance liquid chromatography (RP-HPLC). A total of 334 unique <i>N</i>-glycosite-containing peptides from 153 <i>N</i>-glycoproteins were identified, of which 82 <i>N</i>-glycosite-containing peptides showed significant changes after 12 days of incubation. The varied proteome was mainly involved with antibacterial, ionic binding, cell proliferation, and embryonic development, while the different degrading and/or absorbing priorities of egg proteins were proposed. This study provides substantial insight into the effects of <i>N</i>-glycoprotein variations on the utilization of egg proteins by chicken embryo during incubation.