Research Note: Integrated proteomic analyses of chicken egg yolk granule
ABSTRACT: Chicken egg yolk granules (EYG) were the precipitated component of egg yolk after water dilution and centrifugation. Compared with egg yolk, EYG are rich in proteins, phospholipids, and minerals. In this study, an integrated proteomic analysis was carried out to in-depth mapping of the pro...
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Format: | Article |
Language: | English |
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Elsevier
2023-07-01
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Series: | Poultry Science |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S003257912300233X |
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author | Jiale Sui Jing Xiao Xinping Chang Hongliang Ye Yisha Xu Jinqiu Wang Fang Geng |
author_facet | Jiale Sui Jing Xiao Xinping Chang Hongliang Ye Yisha Xu Jinqiu Wang Fang Geng |
author_sort | Jiale Sui |
collection | DOAJ |
description | ABSTRACT: Chicken egg yolk granules (EYG) were the precipitated component of egg yolk after water dilution and centrifugation. Compared with egg yolk, EYG are rich in proteins, phospholipids, and minerals. In this study, an integrated proteomic analysis was carried out to in-depth mapping of the proteome, phosphoproteome, and N-glycoproteome of EYGs. After hydrolysis of the EYG total protein, the hydrolyzed peptides or the enriched phosphopeptides/glycopeptides were identified by liquid chromatography-tandem mass spectrometry. A total of 125 phosphorylation sites from 36 phosphoproteins and 244 N-glycosylation sites from 100 N-glycoproteins were identified in EYG. All 3 vitellogenins (precursors of egg yolk high-density lipoprotein) were heavily phosphorylated and N-glycosylated, of which 37 phosphorylation sites and 32 N-glycosylation sites were identified on vitellogenins-2. A Total of 30 N-glycosylation sites were identified on apolipoprotein-B (precursor of egg yolk low-density lipoprotein), but no phosphorylation site was identified. These phosphorylation and N-glycosylation of EYG proteins provide new insights for understanding the assembly structure and functional characteristics of EYG, thus contributing to its development and utilization. |
first_indexed | 2024-03-13T05:03:40Z |
format | Article |
id | doaj.art-532e316c28704a1f983e3d0a2cd27d78 |
institution | Directory Open Access Journal |
issn | 0032-5791 |
language | English |
last_indexed | 2024-03-13T05:03:40Z |
publishDate | 2023-07-01 |
publisher | Elsevier |
record_format | Article |
series | Poultry Science |
spelling | doaj.art-532e316c28704a1f983e3d0a2cd27d782023-06-17T05:17:20ZengElsevierPoultry Science0032-57912023-07-011027102711Research Note: Integrated proteomic analyses of chicken egg yolk granuleJiale Sui0Jing Xiao1Xinping Chang2Hongliang Ye3Yisha Xu4Jinqiu Wang5Fang Geng6Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaInstitute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaInstitute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaInstitute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaInstitute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaInstitute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaCorresponding author:; Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaABSTRACT: Chicken egg yolk granules (EYG) were the precipitated component of egg yolk after water dilution and centrifugation. Compared with egg yolk, EYG are rich in proteins, phospholipids, and minerals. In this study, an integrated proteomic analysis was carried out to in-depth mapping of the proteome, phosphoproteome, and N-glycoproteome of EYGs. After hydrolysis of the EYG total protein, the hydrolyzed peptides or the enriched phosphopeptides/glycopeptides were identified by liquid chromatography-tandem mass spectrometry. A total of 125 phosphorylation sites from 36 phosphoproteins and 244 N-glycosylation sites from 100 N-glycoproteins were identified in EYG. All 3 vitellogenins (precursors of egg yolk high-density lipoprotein) were heavily phosphorylated and N-glycosylated, of which 37 phosphorylation sites and 32 N-glycosylation sites were identified on vitellogenins-2. A Total of 30 N-glycosylation sites were identified on apolipoprotein-B (precursor of egg yolk low-density lipoprotein), but no phosphorylation site was identified. These phosphorylation and N-glycosylation of EYG proteins provide new insights for understanding the assembly structure and functional characteristics of EYG, thus contributing to its development and utilization.http://www.sciencedirect.com/science/article/pii/S003257912300233Xegg yolkLC-MS/MSproteomephosphorylationN-glycosylation |
spellingShingle | Jiale Sui Jing Xiao Xinping Chang Hongliang Ye Yisha Xu Jinqiu Wang Fang Geng Research Note: Integrated proteomic analyses of chicken egg yolk granule Poultry Science egg yolk LC-MS/MS proteome phosphorylation N-glycosylation |
title | Research Note: Integrated proteomic analyses of chicken egg yolk granule |
title_full | Research Note: Integrated proteomic analyses of chicken egg yolk granule |
title_fullStr | Research Note: Integrated proteomic analyses of chicken egg yolk granule |
title_full_unstemmed | Research Note: Integrated proteomic analyses of chicken egg yolk granule |
title_short | Research Note: Integrated proteomic analyses of chicken egg yolk granule |
title_sort | research note integrated proteomic analyses of chicken egg yolk granule |
topic | egg yolk LC-MS/MS proteome phosphorylation N-glycosylation |
url | http://www.sciencedirect.com/science/article/pii/S003257912300233X |
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