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Tytuł pozycji:

Ampholine immobilized polymer microspheres for increasing coverage of human urinary proteome.

Tytuł:
Ampholine immobilized polymer microspheres for increasing coverage of human urinary proteome.
Autorzy:
Deng N; Zhengzhou Tobacco Research Institute of CNTC, Zhengzhou, 450001, China; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Chen Y; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China; Mérieux Nutrisciences (China), Ningbo, 315040, China.
Liang Z; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Bian Y; Medical Research Center, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, 450052, China.
Wang B; Zhengzhou Tobacco Research Institute of CNTC, Zhengzhou, 450001, China.
Sui Z; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Zhang X; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Yang K; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Zhang L; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China. Electronic address: .
Zhang Y; Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Science, Dalian, 116023, China.
Źródło:
Talanta [Talanta] 2020 Aug 01; Vol. 215, pp. 120931. Date of Electronic Publication: 2020 Mar 17.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Publication: Amsterdam : Elsevier
Original Publication: Oxford : Pergamon Press
MeSH Terms:
Microspheres*
Glycopeptides/*urine
Glycoproteins/*urine
Polymers/*chemistry
Proteome/*analysis
Humans ; Molecular Structure ; Polyamines/chemistry
Contributed Indexing:
Keywords: Fractionation; Functionalized polymer microspheres; Sample treatment; Urine proteome
Substance Nomenclature:
0 (Glycopeptides)
0 (Glycoproteins)
0 (Polyamines)
0 (Polymers)
0 (Proteome)
37348-94-0 (Ampholine)
Entry Date(s):
Date Created: 20200422 Date Completed: 20201208 Latest Revision: 20201214
Update Code:
20240105
DOI:
10.1016/j.talanta.2020.120931
PMID:
32312467
Czasopismo naukowe
Urinary proteome, as an important component of body fluid proteome, could reflect kidney, urogenital tract function and pathological changes of human organs. This study reports a convenient strategy for urine proteome analysis through ampholine immobilized polymer microsphere (ampholine@PM) fractionation strategy. After ampholine@PM treatment, 16,543 unique peptides corresponding to 2173 non-redundant urinary proteins were identified, while only 856 proteins, corresponding to 3524 peptides were identified in the crude urine sample. The number of proteins and peptides was increased by 1.54 and 3.69 times, respectively. 31 urinary candidate biomarkers have also been identified (17 candidate biomarkers of glomerular injury and 14 candidate biomarkers of tubular injury), showing the potential of our strategy in urinary biomarker discovery study. In additional to the urine proteome, N-glycoproteome analysis was also performed after ampholine@PM fractionation followed by the N-glycopeptides enrichment. The number was increased from 144 to 281 for N-glycoproteins, 261 to 709 for N-glycopeptides, and 226 to 493 for N-glycosylation sites, after ampholine@PM treatment. Based on the significant increase on the identified N-glycoprotein number, ampholine@PM fractionation strategy also offered a beneficial tool for the post translational modification analysis of urine proteome.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 Elsevier B.V. All rights reserved.)

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