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The impact of protein exclusion on the purity performance of ion exchange resins
Author(s) -
Zeid J.,
Harinarayan C.,
van Reis R.
Publication year - 2008
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22101
Subject(s) - dbc , impurity , chemistry , chromatography , conductivity , size exclusion chromatography , chinese hamster ovary cell , ion exchange , analytical chemistry (journal) , chemical engineering , ion , materials science , organic chemistry , enzyme , biochemistry , cmos , engineering , receptor , optoelectronics
Dynamic binding capacity (DBC) decreases with increasing conductivity in the equilibrium regime for ion exchange chromatography. An exclusion regime has been demonstrated in ion exchange resins where DBC increases with increasing conductivity and decreasing protein charge. The purpose of this work was to examine the impact of the exclusion regime on impurity removal. Resin performance was evaluated based on dynamic binding capacities and purity within the exclusion and equilibrium regimes. The results revealed that Chinese hamster ovary proteins (CHOP), a major impurity, exhibit similar exclusion trends as the MAb proteins. The results further the understanding of the exclusion regime and its impact on product purity, a critical area for IEX development and optimization. Biotechnol. Bioeng. 2009; 102: 971–976. © 2008 Wiley Periodicals, Inc.