Electrochemical analysis of Os(VI)-modified glycoproteins and label-free glycoprotein detection eluted from lectin capillary column

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F17%3A00476223" target="_blank" >RIV/68081707:_____/17:00476223 - isvavai.cz</a>

Alternative codes found

RIV/68081715:_____/17:00476223

Result on the web

<a href="http://dx.doi.org/10.1016/j.electacta.2017.04.045" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2017.04.045</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2017.04.045" target="_blank" >10.1016/j.electacta.2017.04.045</a>

Result language

angličtina

Original language name

Electrochemical analysis of Os(VI)-modified glycoproteins and label-free glycoprotein detection eluted from lectin capillary column

Original language description

Earlier we showed that using Os(VI) temed complex, glycans can be modified directly in glycoproteins and detected voltammetrically at mu M concentrations at carbon electrodes. Here we used Os(VI) 2,2'-bipyridine for modification of ribonucleases and Hg electrodes for voltammetric detection. We show that glycosylated RNase B produced electrocatalytic signal (after separation from the reaction mixture) at pM concentrations while non-glycosylated RNase A yielded negligible signal under the same conditions. Using Os(VI) temed and carbon electrodes voltammetric detection was less sensitive but allowed detection of RNase B in an excess of non-glycosylated protein, directly in the reaction mixture. We also showed that the constant current chronopotentiometric stripping (CPS) peak H (which is due to the ability of some amino acid residues in proteins to catalyze hydrogen evolution at Hg electrodes) could be used for protein structure-sensitive analysis at mercury electrodes. Using this peak, here we show that glycosylation of RNase stabilizes its molecule at the electrode. On the other hand, Os(VI) temed modification results in destabilization of this surface-attached protein. Peak H was also used for detection of RNase B separated from a large excess of non-glycosylated proteins on a lectin (concanavalin A) monolithic flow-through column. (C) 2017 Elsevier Ltd. All rights reserved.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Project

<a href="/en/project/GA15-15479S" target="_blank" >GA15-15479S: New tools for research and diagnostics of diseases. Microfluidic reactors and electrochemistry for analysis of proteins and their glycosylation.</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Electrochimica acta

ISSN

0013-4686

e-ISSN

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Volume of the periodical

239

Issue of the periodical within the volume

JUN 2017

Country of publishing house

GB - UNITED KINGDOM

Number of pages

6

Pages from-to

10-15

UT code for WoS article

000401114000002

EID of the result in the Scopus database

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