Article ID Journal Published Year Pages File Type
594857 Colloids and Surfaces A: Physicochemical and Engineering Aspects 2011 5 Pages PDF
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 KD 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.

Related Topics
Physical Sciences and Engineering Chemical Engineering Colloid and Surface Chemistry
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