Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10559801 | Talanta | 2011 | 5 Pages |
Abstract
To evaluate protein-protein interactions, a new voltammetric method was developed using a protein labeled with an electroactive compound. Concanavalin A (ConA), which is a lectin, recognizes α-mannose residues. Because the ConA was to be bound to ovalbumin (OVA), which has a high-mannose sugar chain, ConA labeled with daunomycin was prepared as the probe to monitor the binding. The binding to OVA was caused by the label modification of the ConA. As a result, the electrode response of the labeled ConA decreased as the OVA concentration increased. The electrode response of the labeled ConA was linearly over the range of 1.5 Ã 10â10 and 1.5 Ã 10â9 M OVA. The relative standard deviation of 1.5 Ã 10â8 M labeled ConA and 1.5 Ã 10â10 M OVA was 6.9% (n = 5). The labeled ConA-OVA binding could then be conveniently monitored based on the change in response. In contrast, interactions between the labeled ConA and a protein with no specific sugar chain also were investigated. Incubation scarcely influenced the peak current of the labeled ConA. When several concentrations of OVA were added to a serum, good recovery determined it. Consequently, this method could be applied to the measurement of protein-protein interactions.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Kazuharu Sugawara, A. Yugami, Toshihiko Kadoya, Kohei Hosaka,