Počet záznamů: 1

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

SYSNO ASEP	0476223
Druh ASEP	J - Článek v odborném periodiku
Zařazení RIV	J - Článek v odborném periodiku
Poddruh J	Článek ve WOS
Název	Electrochemical analysis of Os(VI)-modified glycoproteins and label-free glycoprotein detection eluted from lectin capillary column
Tvůrce(i)	Trefulka, Mojmír (BFU-R)_{RID, ORCID} Dorčák, Vlastimil (BFU-R)_{RID, ORCID} Křenková, Jana (UIACH-O)_{RID, ORCID} Foret, František (UIACH-O)_{RID, ORCID} Paleček, Emil (BFU-R)_{RID, ORCID}
Celkový počet autorů	5
Zdroj.dok.	Electrochimica acta. - : Elsevier - ISSN 0013-4686 Roč. 239, JUN 2017 (2017), s. 10-15
Poč.str.	6 s.
Forma vydání	Tištěná - P
Jazyk dok.	eng - angličtina
Země vyd.	GB - Velká Británie
Klíč. slova	voltammetric determination ; modified electrodes ; high-sensitivity ; concanavalin-a
Vědní obor RIV	CG - Elektrochemie
Obor OECD	Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Vědní obor RIV – spolupráce	Ústav analytické chemie - Analytická chemie, separace
CEP	GA15-15479S GA ČR - Grantová agentura ČR
Institucionální podpora	BFU-R - RVO:68081707 ; UIACH-O - RVO:68081715
UT WOS	000401114000002
DOI	10.1016/j.electacta.2017.04.045
Anotace	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.
Pracoviště	Biofyzikální ústav
Kontakt	Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244
Rok sběru	2018

Počet záznamů: 1