期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1216, 期 45, 页码 7950-7956出版社
ELSEVIER
DOI: 10.1016/j.chroma.2009.09.040
关键词
Protein; Cation exchange; Monoclonal antibody; Dynamic binding capacity; Linear gradient elution
This work provides a broad survey of binding and elution behavior of proteins on strong cation exchangers. Four proteins comprising two monoclonal antibodies, lysozyme, and cytochrome c were used as models in the investigation. Seven chromatography resins with different base matrices were compared. Dynamic binding capacity as a function of salt concentration was examined for a monoclonal antibody and lysozyme. Elution behavior as a function of gradient slope was modeled to determine the characteristic charge, essentially a measure of the number of sites involved in binding, for each protein on each resin. Trends with respect to dynamic binding capacity and elution behavior are analyzed and discussed. (C) 2009 Published by Elsevier B.V.
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