Abstract

The rapid progress of biotechnology, immunology and molecular biology are requiring antibodies with higher purity and stronger activity. Therefore, the development of efficient technology, which is suitable for large-scale purification of antibodies at low cost, becomes much more urgent. In this study, we presented a novel method to isolate immunoglobulin G from human serum based on the utilization of thiophilic magnetic polymer beads. Micron-sized magnetic beads with paramagnetic properties were synthesized by microsuspension polymerization in the presence of modified magnetite. After the thiophilic ligand of 2-mercaptonicotinic acid was modified on the surface, these magnetic beads exhibited a strong specificity towards immunoglobulin G in a salt-independent manner. Then, antibodies could be directly isolated from human serum in batch-wise mode with the assistance of magnetic decantation. The purity of the isolated antibody exceeded 94%. Because isolation was performed in physiological conditions, bioactivity of the antibody was fully preserved (>99%). Prominent advantages of this method, such as strong specificity, rapid processing, mild conditions, conventional equipment and excellent reusability, make this non-chromatographic technology embody great potentialities to isolate the antibodies on a large scale.

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