Comparison of three distinct ELLA protocols for determination of apparent affinity constants between Con A and glycoproteins

Colloids and Surfaces. B, Biointerfaces
D MislovicováJan Tkac

Abstract

A procedure for determination of apparent affinity constants K(D)(app) between Concanavalin A (Con A) and naturally d-mannose containing glycoproteins using enzyme-linked lectin assay (ELLA) is reported. Three distinct ELLA protocols are compared to each other with 3 different fitting models used (Liliom, Hill with and without a cooperativity factor). The glycoproteins were physisorbed on a highly charged polystyrene solid surface of immunoassay plates and the amount of lectin bound to the glycoproteins was determined by photometry. The interactions of Con A with five mannose-containing glycoproteins, invertase (INV), glucoamylase (GA), glucose oxidase (GOx), ovalbumin (OVA), and transferrin (TRF) were quantified with apparent affinity constant being in the range 2×10(-7) to 9×10(-6)M. The strength of interaction between Con A and glycoproteins is discussed on the basis of glycan structure/exposure on the protein backbone for each glycoprotein.

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Citations

Nov 8, 2013·Molecular & Cellular Proteomics : MCP·Eliel Ruiz-MayJocelyn K C Rose
Jan 1, 2013·Mikrochimica Acta·Tomáš BertókJan Tkac
Feb 1, 2014·Molecular & Cellular Proteomics : MCP·Eliel Ruiz-MayJocelyn K C Rose

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