This work presents data on human imrnunoglobulin G (HlgG) adsorption onto L-arginine ligand attached poly(GMA/MMA/EGDMA)-based affinity beads which were synthesized from methyl methacrylate (NUVIA) and glycidiyl methacrylate (GMA) in the presence of a crosslinker (i.e., ethylene glycol dimethacrylate; EGDMA) by suspension polymerization. The epoxy groups of the poly(GMA/NMA/ EGDMA) beads were converted into amino groups after reaction with ammonia or 1,6-diaminohexane (i.e., spacer-arm). With L-arginine as a ligand, it was covalently immobilized on the an-dnated (poly(GMA/MMA/EGDMA)AA) and/or the spacer-arm attached (poly(GMA/NMA/ EGDM.A)-SA) beads, using glutaric dialdehyde as a coupling agent. Both affinity poly(GMA/MMA/EGDMA)-based beads were used in HlgG adsorption/desorption studies under defined pH, ionic strength, or temperature conditions in a batch reactor, using acid-treated poly(GMA/MMA/EGDMA) beads as a control system. The poly(GMA/MMA/EGDMA)-SA affinity beads resulted in an increase in the adsorption capacity to HlgG compared with the aminated counterpart (i.e., poly(GMA/MMA/EGDMA)-AA). The maximum adsorption capacities of the poly(GMA/MMA/EGDMA)-AA and poly(GMA/MNA/EGDMA)-SA affinity beads were found to be 112.36 and 142 mg g(-1), and the affinity constants (K-d), evaluated by the Langmuir model, were 2.48 x 10(-7) and 6.98 x 10(-7) M, respectively. Adsorption capacities of the poly(GMA/MMA/EGDMA)-AA and poly(GMA/MMA/EGDMA)-SA were decreased with HIgG by increasing the ionic strength adjusted with NaCl. Adsorption kinetic of HIgG onto both affinity adsorbents was analyzed with first-and second-order kinetic equations. The first-order equation fitted well with the experimental data. (c) 2007 Wiley Periodicals, Inc.