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首页> 外文期刊>Journal of Applied Polymer Science >Effect of Adsorbed Metal Ions and Buffer Nature on IgG Separation from Human Plasma by Column Chromatography Using an Ion Exchange Resin, Amberlite IRC-718
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Effect of Adsorbed Metal Ions and Buffer Nature on IgG Separation from Human Plasma by Column Chromatography Using an Ion Exchange Resin, Amberlite IRC-718

机译：使用离子交换树脂Amberlite IRC-718的柱色谱法分析吸附的金属离子和缓冲液性质对人血浆IgG分离的影响

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摘要

Fractionation of human plasma on ion exchanger resin was performed on Amberlite IRC-718 saturated with metal ions. Depletion of human immunoglobulin G was carried out by column chromatography using Tris-HCl, pH 7 at different concentrations. Results showed that, when Cu+2 and Ni+2 were adsorbed on the resin, one or two fractions of purified IgG were obtained, respectively. Whereas Fe+2 and Zn+2, both retain IgG and serum albumin or serum albumin alone. Furthermore, the Ni+2- resin retention of serum proteins is too strong that the use of 700 mMTris-HCl cannot liberate any other proteins than nonadsorbed serum albumin. In conclusion, this investigation demonstrates that immobilized metal ion affinity chromatography with Cu2+, Ni2+, and Fe2+ immobilized on Amberlite IRC-718 has the potential to be developed as part of a process to purify IgG out of untreated human plasma as acceptable adsorption and elution levels of IgG could be achieved.
机译：在用金属离子饱和的Amberlite IRC-718上，在离子交换树脂上分离人类血浆。通过使用Tris-HCl，pH 7，不同浓度的柱色谱法进行人免疫球蛋白G的消耗。结果表明，当将Cu + 2和Ni + 2吸附到树脂上时，分别获得了一到两份纯化的IgG。 Fe + 2和Zn + 2均保留IgG和血清白蛋白或血清白蛋白。此外，血清蛋白的Ni + 2-树脂保留力太强，以至于使用700 mMTris-HCl不能释放除未吸附的血清白蛋白以外的任何其他蛋白。总之，这项研究表明，固定在Amberlite IRC-718上的具有Cu2 +，Ni2 +和Fe2 +的固定化金属离子亲和色谱有可能被开发为从可接受的吸附和洗脱水平中纯化未经处理的人血浆中的IgG的方法的一部分。可以达到IgG的浓度。

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