【摘 要】
：
A robust and scalable purification process was developed to quickly generate antibody of high purity and sufficient quantity from glycoengineered Pichia pas
【机 构】
：
Director of Glycoprotein Purification and Bioanalytics GlycoFi,Inc. A Wholly Owned Subsidiary of Mer
论文部分内容阅读
A robust and scalable purification process was developed to quickly generate antibody of high purity and sufficient quantity from glycoengineered Pichia pastoris fermentation.Protein A affinity chromatography was used to capture the antibody from fermentation supernatant.A pH gradient elution was applied to the Protein A column to prevent antibody precipitation at low pH.Antibody from Protein A chromatography contained some product related impurities, which were the misassembling of cleaved heavy chain, heavy chain and light chain.It also had some process related impurities, including Protein A residues, endotoxin, host cell DNA and proteins.Cation exchange chromatography with optimal NaCl gradient at pH 4.5-6.0 efficiently removed these product and process related impurities.The antibody from glycoengineered P.pastoris was comparable to its commercial counterpart in heterotetramer folding, physical stability and binding affinity.
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