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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorYu, Y.
dc.contributor.authorZang, N.
dc.contributor.authorZhang, F.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorZhang, H.
dc.date2017
dc.date.accessioned2022-06-21T17:21:36Z
dc.date.available2022-06-21T17:21:36Z
dc.date.issued2017
dc.identifier.citationProteome analysis and selenium-binding peptide identification on proteins sequentially extracted from loach (Misgurnus anguillicaudatus), Y. Yu, N. Zang, F. Zhang, R. J. Linhardt, H. Zhang, Biochemistry and Physiology, 6, 1000214, 2017.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5079
dc.identifier.urihttp://doi.org/10.4172/2168-9652.1000214
dc.descriptionProteome analysis and selenium-binding peptide identification on proteins sequentially extracted from loach (Misgurnus anguillicaudatus)
dc.description.abstractLoach (Misgurnus anguillicaudatus) is known as a selenium-rich aquatic product. In present study, a sequential extraction method was applied for separation of water, salt and alkali-soluble proteins from loach (Misgurnus anguillicaudatus). The extracted proteins (included 12 water-soluble, 4 salt-soluble and 7 alkali-soluble proteins) were subjected to molecular weight analysis by SDS-PAGE and MALDI-TOF MS. Then, water soluble proteins were chosen for further ion exchange purification after selenium tracking by ICP-MS. The selenium containing peptides in water soluble proteins were identified by ESI-MS. Four proteins including creatine kinase, cytochrome P450 aromatase, beta-actin and glyceraldehyde 3-phosphate dehydrogenase were identified. Among these proteins, two selenium-containing peptides from beta-actin and cytochrome P450 aromatase were identified. The results of proteome analysis provide valuable molecular information of loach proteins. Moreover, it helps to understand the effect of selenium on redox systems in loach and its antioxidant functions.
dc.languageen_US
dc.language.isoENG
dc.publisherBiochemistry & Physiology
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleProteome analysis and selenium-binding peptide identification on proteins sequentially extracted from loach (Misgurnus anguillicaudatus)en_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dcterms.isVersionOfhttp://doi.org/10.4172/2168-9652.1000214
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
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)


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CC BY — Creative Commons Attribution
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution