期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1216, 期 20, 页码 4366-4371出版社
ELSEVIER
DOI: 10.1016/j.chroma.2008.08.047
关键词
Ion exchange chromatography; Protein; Monoclonal antibody; Exclusion mechanism; Ligand density; Pore size; Dynamic binding capacity
资金
- NIGMS NIH HHS [T32 GM008336-21, T32 GM008336-19, T32 GM008336-20] Funding Source: Medline
Dynamic binding capacity (DBC) of a monoclonal antibody on agarose based strong cation exchange resins is determined as a function of resin ligand density, apparent pore size of the base matrix, and protein charge. The maximum DBC is found to be unaffected by resin ligand density, apparent pore size, or protein charge within the tested range. The critical conductivity (conductivity at maximum DBC) is seen to vary with ligand density. It is hypothesized that the maximum DBC is determined by the effective size of the proteins and the proximity to which they can approach one another. Once a certain minimum resin ligand density is supplied, additional ligand is not beneficial in terms of resin capacity. Additional ligand can provide flexibility in designing ion exchange resins for a particular application as the critical conductivity could be matched to the feedstock conductivity and it may also affect the selectivity. (C) 2008 Elsevier B.V. All rights reserved.
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