Abstract
Iminodiacetic acid (IDA)-functionalized adsorbents have attracted increasing interest in recent years for immobilized metal-affinity chromatography (IMAC). In this study, IDA was covalently attached to nonporous monosize poly(glycidyl methacrylate) [poly(GMA)] beads (1.6 μm in diameter). Cu2+ ions were chelated via IDA groups for affinity depletion of immunoglobulin G (IgG) from human serum. The monosize poly(GMA) beads were characterized by scanning electron microscopy. The Cu2+-chelated beads (628 μmol/g) were used in the IgG adsorption−elution studies. Studies to determine the effects of IgG concentration, pH, and temperature on the adsorption efficiency of Cu2+-chelated beads were performed in a batch system. Nonspecific binding of IgG to monosize beads in the absence of Cu2+ ions was very low (0.45 mg/g). The IgG adsorption to chelated Cu2+ ions was 171.2 mg/g. The equilibrium IgG adsorption increased with increasing temperature. The negative change in Gibbs free energy (ΔGo < 0) indicated that the a...
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