Monoclonal antibody purification by ceramic hydroxyapatite chromatography
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Updated: May 3, 2026

Purification and Analytics of a Monoclonal Antibody from Chinese Hamster Ovary Cells Using an Automated Microbioreactor System
Published on: May 1, 2019
Larry J Cummings1, Russell G Frost, Mark A Snyder
1Bio-Rad Laboratories, Inc., Hercules, CA, USA.
Abstract:
Hydroxyapatite chromatography is shown to be an excellent method for chromatographically purifying monoclonal antibodies (Mab). Mab contained in eluates from Protein A columns was partially purified on ceramic hydroxyapatite (CHT™) Type I, 40 μm ceramic hydroxyapatite using two scouting methods which provide milligram amounts of Mab typical at laboratory scale. The result from one of the scouting methods was optimized to obtain a high concentration of purified Mab with acceptable clearance of cell culture impurities. Several techniques (linear phosphate screening, linear alkaline salt screening, and two alkaline salt step gradients) are described for obtaining high concentrations of purified Mab in a lab-scale CHT chromatography column.
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