著者

Naoki NISHIMURA Toyohiro NAITO Takuya KUBO Koji OTSUKA

出版者

The Society for Chromatographic Sciences

雑誌

CHROMATOGRAPHY (ISSN:13428284)

巻号頁・発行日

vol.39, no.3, pp.113-118, 2018-10-20 (Released:2018-11-08)

参考文献数

36

被引用文献数

6 4

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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.