Electrochemical sensing of concanavalin A and ovalbumin interaction in solution
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
27543018
DOI
10.1016/j.aca.2016.06.055
PII: S0003-2670(16)30818-2
Knihovny.cz E-resources
- Keywords
- Concanavalin A, Constant current chronopotentiometric stripping, Lectin-glycoprotein interactions, Mercury electrodes, Ovalbumin, Protein-protein interactions,
- MeSH
- Canavalia chemistry MeSH
- Electrochemical Techniques * MeSH
- Concanavalin A analysis MeSH
- Chickens MeSH
- Models, Molecular MeSH
- Ovalbumin analysis MeSH
- Solutions MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Concanavalin A MeSH
- Ovalbumin MeSH
- Solutions 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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