Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F18%3A00108842" target="_blank" >RIV/00216224:14310/18:00108842 - isvavai.cz</a>
Alternative codes found
RIV/68081715:_____/18:00489967
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0021967318306137" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0021967318306137</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.chroma.2018.05.030" target="_blank" >10.1016/j.chroma.2018.05.030</a>
Alternative languages
Result language
angličtina
Original language name
Multi-charged labeling of oligosaccharides and N-linked glycans by hexahistidine-based tags for capillary electrophoresis-mass spectrometry analysis
Original language description
The labeling by amino acids and peptides was investigated for sensitive and fast analyses of oligosaccharides and N-linked glycans by capillary electrophoresis-mass spectrometry (CE-MS). Peptide tags with a various number of histidine residues were tested for maltooligosaccharide labeling in order to investigate the effect of the size of labels and a number of charges on CE-MS analysis. Nevertheless, the reductive amination labeling of N-linked glycans by a hexahistidine tag resulted in a multiple products formation, therefore a peptide tag was modified by hydrazine functionality in order to perform labeling by hydrazone formation chemistry. This labeling approach significantly improved sensitivity with LOD of labeled maltopentaose determined to be 40 nmol/L and also significantly reduced separation time of neutral maltooligosaccharides and N-linked glycans released from bovine ribonuclease B. Furthermore, the labeling by this multi-cationic peptide hydrazine tag also allowed performing analysis of acidic glycans by CE-MS in a positive ion mode as demonstrated by separation of sialylated N-linked glycans released from bovine fetuin.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Chromatography A
ISSN
0021-9673
e-ISSN
1873-3778
Volume of the periodical
1560
Issue of the periodical within the volume
JUL
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
6
Pages from-to
91-96
UT code for WoS article
000434902900012
EID of the result in the Scopus database
2-s2.0-85046873722