Protein Crystallization for Antibody Purification
Author Information
Author(s): Zang Yuguo, Kammerer Bernd, Eisenkolb Maike, Lohr Katrin, Kiefer Hans
Primary Institution: Institute of Pharmaceutical Biotechnology, Biberach University of Applied Sciences, Biberach, Germany
Hypothesis
Can protein crystallization be effectively used as a purification step in the downstream processing of therapeutic antibodies?
Conclusion
Protein crystallization can achieve over 90% purity for monoclonal antibodies, but the yield from culture supernatant remains low.
Supporting Evidence
- Crystallization conditions were established for an intact monoclonal IgG4 antibody.
- Purification efficiency of the crystallization step was over 95% for model protein contaminants.
- No measurable loss of Fc-binding activity was observed in the crystallized antibody.
Takeaway
Scientists are trying to use a method called crystallization to clean up antibodies, making them very pure, but it's still tricky to get a lot of them at once.
Methodology
The study involved optimizing crystallization conditions for an IgG4 antibody using vapor diffusion and microbatch techniques.
Limitations
The yield of crystallized antibodies from culture supernatant was low, and the crystallization process took several days.
Digital Object Identifier (DOI)
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