Electrochemical sensing of concanavalin A and ovalbumin interaction in solution
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
27543018
DOI
10.1016/j.aca.2016.06.055
PII: S0003-2670(16)30818-2
Knihovny.cz E-zdroje
- Klíčová slova
- Concanavalin A, Constant current chronopotentiometric stripping, Lectin-glycoprotein interactions, Mercury electrodes, Ovalbumin, Protein-protein interactions,
- MeSH
- Canavalia chemie MeSH
- elektrochemické techniky * MeSH
- konkanavalin A analýza MeSH
- kur domácí MeSH
- molekulární modely MeSH
- ovalbumin analýza MeSH
- roztoky MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- konkanavalin A MeSH
- ovalbumin MeSH
- roztoky MeSH
In an attempt to develop a label- and reagent-free electrochemical method for the detection of lectin-glycoprotein interactions, we tested lectin-concanavalin A (ConA), glycoprotein-ovalbumin (Ova) and their complex using chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode. Incubation of ConA with Ova resulted in an increase of the CPS peak H of the complex as compared to the CPS peaks of individual Ova and ConA proteins. Qualitatively similar results were obtained with other glycoprotein-lectin couples (ConA-RNase B and lectin from Sambucus nigra-fetuin). Using the CPS method, we were able to follow the course of complex formation in solution. Comparable responses of Ova, ConA and ConA-Ova complex were obtained not only at the mercury electrode but also with solid amalgam electrodes, which are more suitable for parallel analysis. It can be anticipated that electrochemical methods, namely CPS, will find application in glycomics and proteomics.
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