Cryogels with embedded natural adsorbent are new trend of chromatographic media for separation of biomolecules. In this report, experimental determination of immunoglobulin G (IgG) purification by Cu2+-attached pumice particles unified cryogel (Cu2+-PPUC) was performed. For this purpose, after preparation of Cu2+-attached pumice particles, they were unified with 2-hydroxyethyl methacrylate monomers to produce Cu2+-PPUC through polymerization of gel-forming precursors at subzero temperatures. IgG separation experiments were accomplished in a continuous column system. The highest binding capacity (596.8 mg/g) was obtained by working with 0.02 M phosphate buffer at pH 6.0. The chemical analysis of pumice was examined by X-ray fluorescence spectrometer. Scanning electron microscopy was performed to identify the morphology of Cu2+-PPUC. Langmuir adsorption model was best fitted to interaction when compared to Freundlich model. Temkin model was utilized to characterize adsorption, energetically. Purification ability of Cu2+-PPUC for IgG was shown with high selectivity via reducing SDS–PAGE electrophoresis.

中文翻译：

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浮石颗粒界面：免疫球蛋白 G 纯化的案例研究

嵌入天然吸附剂的冷冻凝胶是分离生物分子的色谱介质的新趋势。在本报告中，通过 Cu2+ 附着的浮石颗粒统一冷冻凝胶 (Cu2+-PPUC) 进行了免疫球蛋白 G (IgG) 纯化的实验测定。为此，在制备附有 Cu2+ 的浮石颗粒后，将它们与甲基丙烯酸 2-羟乙酯单体结合，通过在零下温度下聚合凝胶形成前体来生产 Cu2+-PPUC。IgG 分离实验在连续柱系统中完成。通过使用 pH 6.0 的 0.02 M 磷酸盐缓冲液获得最高结合容量 (596.8 mg/g)。浮石的化学分析采用X射线荧光光谱仪进行检测。进行扫描电子显微镜检查以鉴定 Cu2+-PPUC 的形态。与 Freundlich 模型相比，Langmuir 吸附模型最适合相互作用。Temkin 模型被用来表征吸附，能量。Cu2+-PPUC 对 IgG 的纯化能力通过还原 SDS-PAGE 电泳显示出高选择性。