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dc.contributor.authorLiu, Zhangguo
dc.contributor.authorSong, Lingzi
dc.contributor.authorLu, Lizhi
dc.contributor.authorZhang, Xianfu
dc.contributor.authorZhang, Fuming
dc.contributor.authorWang, Kehua
dc.contributor.authorLinhardt, Robert J.
dc.date2017
dc.date.accessioned2022-06-27T16:01:10Z
dc.date.available2022-06-27T16:01:10Z
dc.date.issued2017-09-07
dc.identifier.citationComparative proteomics of matrix fractions between pimpled and normal chicken eggshells, Z. Liu, L. Song, L. Lu, X. Zhang, F. Zhang, K. Wang, R. J. Linhardt, Journal of Proteomics, 167, 1–11, 2017.
dc.identifier.issn18767737
dc.identifier.issn18743919
dc.identifier.urihttps://doi.org/10.1016/j.jprot.2017.07.015
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5616
dc.descriptionJournal of Proteomics, 167, 1–11
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractEggshell matrix can be dissociated into three matrix fractions: acid-insoluble matrix (M1), water-insoluble matrix (M2) and acid-water facultative-soluble matrix (M3). Matrix fractions from pimpled and normal eggshells were compared using label-free proteomic method to understand the differences among three matrix fractions and the proteins involved with eggshell quality. A total of 738 and 600 proteins were identified in the pimpled and normal calcified eggshells, respectively. Both eggshells showed a combined proteomic inventory of 769 proteins. In the same type of eggshell, a high similarity was present in the proteomes of three matrix fractions. These triply overlapped common proteins formed the predominant contributor to proteomic abundance in the matrix fractions. In each matrix fraction and between both eggshell models, normal and pimpled eggshells, a majority of the proteomes of the fractions were commonly observed. Forty-two common major proteins (iBAQ-derived abundance ≥ 0.095% of proteomic abundance) were identified throughout the three matrix fractions and these proteins might act as backbone constituents in chicken eggshell matrix. Finally, using 1.75-fold as up-regulated and using 0.57-fold as down-regulated cutoff values, twenty-five differential major proteins were screened and they all negatively influence and none showed any effect on eggshell quality. Overall, we uncovered the characteristics of proteomics of three eggshell matrix fractions and identified candidate proteins influencing eggshell quality. The next research on differential proteins will uncover the potential mechanisms underlying how proteins affect eggshell quality.
dc.description.sponsorshipAgro-Industry R and D Special Fund of China
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.jprot.2017.07.015
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Proteomics
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleComparative proteomics of matrix fractions between pimpled and normal chicken eggshells
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.jprot.2017.07.015
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.jprot.2017.07.015
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages1-11
rpi.description.volume167


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