Proteome analysis and selenium-binding peptide identification on proteins sequentially extracted from loach (Misgurnus anguillicaudatus)
Author
Yu, Y.; Zang, N.; Zhang, F.; Linhardt, Robert J.; Zhang, H.Other Contributors
Date Issued
2017Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineeringDegree
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CC 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.; Attribution 3.0 United StatesFull Citation
Proteome 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.Metadata
Show full item recordAbstract
Loach (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.;Description
Proteome analysis and selenium-binding peptide identification on proteins sequentially extracted from loach (Misgurnus anguillicaudatus)Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);Publisher
Biochemistry & PhysiologyRelationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;Access
CC BY — Creative Commons Attribution; A full text version is available in DSpace@RPI; Open Access;Collections
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