Fig. 7
From: Kinetic Analysis of Glycoprotein–Lectin Interactions by Label-Free Internal Reflection Ellipsometry
a–c Affinity chromatography of thyroglobulin on M-LAC, ConA, and WGA, respectively. Chromatographic conditions are described in “Materials and Methods.” Bound thyroglobulin was eluted with solvent B (100 mM acetic acid, pH 4.0), and protein elution was monitored at 280 nm. The quantitation was performed using peak area with 1.6%, 21%, and 55% bound to ConA, WGA, and M-LAC, respectively. d Kinetic data run on LFIRE™ showing the interaction of circulating thyroglobulin with an immobilized spot containing equimolar concentrations of ConA/WGA/jacalin compared to spots containing single lectins, ConA, and WGA. The total binding to the mixed lectin spot is more than twice the amount of binding to ConA. Kinetic fit results show the binding affinity about six times higher for the mixed lectin interaction over ConA and over an order of magnitude over WGA