期刊
CHROMATOGRAPHY
卷 39, 期 3, 页码 113-118出版社
SOC CHROMATOGRAPHIC SCIENCES
DOI: 10.15583/jpchrom.2018.018
关键词
Spongy monolith; Poly(ethylene-co-glycidylmethacrylate); Affinity chromatography; Hydrophobicity; Protein A; IgG
资金
- Japan Society for the Promotion of Science [25620111, 15K13756, 15601162]
- JST CREST, Japan [JPMJCR17H2]
- Grants-in-Aid for Scientific Research [25620111, 15K13756] Funding Source: KAKEN
In this study, we reveal the suppression of non-specific hydrophobic interaction in poly(ethylene-co-glycidylmethacrylate) (PEGM) based spongy monolith (SPM), PEGM-SPM, which has recently be reported as a new platform of separation medium for affinity chromatography in our previous study, by an simple acidic treatment. Additionally, the immobilization procedures of protein-A toward the PEGM-SPM and the separation conditions for immunoglobulin G (IgG) were optimized for further effective affinity separations. As a result of treatment by a mixture of trifluoroacetic acid and acetonitrile, the hydrophobicity was dramatically suppressed in the PEGM-SPM. The optimizations for the density of PEGM in the PEGM-SPM, the protein A immobilization, and the binding/releasing conditions showed that variety of proteins and peptides were not retained on the protein A immobilized spongy column at all while IgG was absolutely separated by a simple stepwise pH gradient condition.
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