Abstract
Recently, the modification of gold surfaces with covalently bound carboxylated dextran was described, for use in biospecific interaction studies in an analytical system based on surface plasmon resonance (SPR). In this study, the antigen binding immunoreactivity of antibodies immobilized on the modified surfaces was investigated with the SPR-based system. Four different monoclonal antibodies specific against the antigens β 2-microglobulin, luteinizing hormone, human transferrin, and immunoglobulin E, were covalently attached by amine coupling to the dextran layer and the antigen binding capacities were evaluated for different amounts of bound antibody. High immunoreactivities were obtained with molar activities ranging from 0.6 to 1.5 over a wide range of surface concentrations. Interaction studies between carboxymethylated dextran surfaces and antibodies showed that, in comparison with unmodified gold surfaces, the modified surface had low nonspecific adsorption and high capacity for antibody immobilization.
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