Abstract
Binding of selected glycoproteins containing α- d-mannose sites (invertase, glucoamylase, transferrin, glucose oxidase, and albumin α- d-mannopyranosylphenyl isothiocyanate) with two lectins selective for α- d-mannose branching glycans, concanavalin A (ConA), and Lens culinaris agglutinin (LCA) was studied on lectin biochips by microfluidic surface plasmon resonance (SPR). Lectin-containing biochips were prepared by covalent immobilization of lectins on a flat carboxymethylated gold surface. Both measurement as well as regeneration conditions were optimized. The determined dissociation constants of lectin–glycoprotein interactions were 10 −5 to 10 −7 mol/l. Dissociation constants K D of studied bindings were estimated by the steady state specific binding models based on both a binding to one site and the multiple binding sites model using Hill slope.
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