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Updated: May 10, 2026
Purification and Analytics of a Monoclonal Antibody from Chinese Hamster Ovary Cells Using an Automated Microbioreactor System
Published on: May 1, 2019
Purification and characterization of rabbit polyclonal immunoglobulin G using DEAE ion-exchange chromatography and
S H S Mariam1, Roslan Noorain1, W S Tan2
1Malaysian Institute of Chemical & Bioengineering Technology, Universiti Kuala Lumpur, Lot 1988 Kawasan Perindustrian Bandar Vendor Taboh Naning, Alor Gajah, Melaka, 78000, Malaysia.
Abstract:
Weak anion-exchange chromatography (AEC) provides a mild alternative to ammonium sulfate (AS) precipitation for antibody purification, but its mechanistic behavior in complex serum systems remains unclear. This study evaluates pH-dependent DEAE flow-through purification of rabbit anti-HBcAg IgG and compares it with AS precipitation. At pH 8.0, DEAE chromatography achieved 94% recovery and 83% purity, consistent with reduced IgG-resin interaction and selective retention of anionic serum proteins. Conductivity profiling showed a 69% reduction in ionic strength relative to AS-treated samples, correlating with improved structural homogeneity. Dynamic light scattering revealed a monomodal ∼10 nm hydrodynamic diameter for DEAE-purified IgG, whereas AS precipitation generated multimodal distributions indicative of aggregation. These results clarify how pH, ionic strength, and protein-protein interactions govern IgG behavior during weak AEC. The findings position DEAE chromatography as a gentle, aggregation-minimizing, and scalable method for producing high-quality polyclonal antibodies for diagnostic applications.
