Purification of Human Antibodies from Transgenic Corn Using Aqueous Two-Phase Systems
A recombinant human antibody expressed in corn was purified using aqueous two-phase extraction. The antibody was an immunoglobulin G fully unglycosylated. Using systems of different compositions and/or pHs in each of one or two partitioning stages followed by one more stage in which the antibody was precipitated at the liquid/liquid interface facilitated the removal of different impurities in each stage. The best system yields a product 72% pure (22-fold purification) with a yield of 49%. The optimum extraction was done in two partitioning stages followed by an interfacial precipitation stage using poly(ethylene)glycol/ potassium phosphate systems. NaCl was added to the first stage to eliminate large molecular weight impurities. The pH in the first stage was kept at 6 but a pH of 8 was used in the second stage and in the precipitation stage.
J. Lee and D. Forciniti, "Purification of Human Antibodies from Transgenic Corn Using Aqueous Two-Phase Systems," Biotechnology Progress, American Institute of Chemical Engineers (AIChE), Jan 2010.
The definitive version is available at http://dx.doi.org/10.1002/btpr.287
Chemical and Biochemical Engineering
Keywords and Phrases
PEG; Antibody; Aqueous Two-phases; Purification
Article - Journal
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