Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00072093" target="_blank" >RIV/00216224:14740/13:00072093 - isvavai.cz</a>
Alternative codes found
RIV/68081715:_____/13:00398549
Result on the web
<a href="http://dx.doi.org/10.1016/j.chroma.2013.10.087" target="_blank" >http://dx.doi.org/10.1016/j.chroma.2013.10.087</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.chroma.2013.10.087" target="_blank" >10.1016/j.chroma.2013.10.087</a>
Alternative languages
Result language
angličtina
Original language name
Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis
Original language description
In this paper, we report on a novel oriented peptide-N-glycosidase F (PNGase F) immobilization approach onto methacrylate based monolithic support for rapid, reproducible and efficient release of the N-linked carbohydrate moieties from glycoproteins. Theglutathione-S-transferase-fusion PNGase F (PNGase F-GST) was expressed in Escherichia coli using regular vector technology. The monolithic pore surface was functionalized with glutathione via a succinimidy1-6-(iodoacetyl-amino)-hexanoate linker and thespecific affinity of GST toward glutathione was utilized for the oriented coupling. This novel immobilization procedure was compared with reductive amination technique commonly used for non-oriented enzyme immobilization via primary amine functionalities. Both coupling approaches were compared using enzymatic treatment of several glycoproteins, such as ribonuclease B, fetuin and immunoglobulin G followed by MALDI/MS and CE-LIF analysis of the released glycans.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
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
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Volume of the periodical
1322
Issue of the periodical within the volume
Dec
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
54-61
UT code for WoS article
000328717200007
EID of the result in the Scopus database
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