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首页> 外文期刊>CHROMATOGRAPHY >Suppression of Hydrophobicity and Optimizations of a Ligand-Immobilization for Effective Affinity Chromatography Using a Spongy Monolith
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Suppression of Hydrophobicity and Optimizations of a Ligand-Immobilization for Effective Affinity Chromatography Using a Spongy Monolith

机译：疏水性的抑制和配体固定化的优化，以利用海绵状整体进行有效亲和色谱

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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.
机译：在这项研究中，我们揭示了基于聚（乙烯-共-缩水甘油甲基丙烯酸甲酯）（PEGM）的海绵状整体结构（SPM）PEGM-SPM中非特异性疏水相互作用的抑制作用，该物质最近被报道为一种新的分离平台在我们以前的研究中，亲和层析是通过简单的酸性处理。此外，针对进一步有效的亲和力分离，优化了将蛋白A固定在PEGM-SPM上的步骤和免疫球蛋白G（IgG）的分离条件。通过用三氟乙酸和乙腈的混合物进行处理的结果，在PEGM-SPM中显着抑制了疏水性。对PEGM-SPM中PEGM密度，蛋白A固定以及结合/释放条件的优化表明，各种蛋白和肽根本没有保留在蛋白A固定的海绵色谱柱上，而IgG通过简单的逐步pH梯度条件。

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