Department of Chemical and Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, S117576 Singapore.
Biotechnol Adv. 2011 Nov-Dec;29(6):840-9. doi: 10.1016/j.biotechadv.2011.07.001. Epub 2011 Jul 7.
Extensive research in the past two decades has led to the realization of Immunoglobulin-M (IgM) as a potential therapeutic and diagnostic agent. In order to fully exploit the potential of IgM, large quantities, in a highly pure and active form, must be available at low cost for performing clinical trials, characterization studies and quantitative-structure activity analyses. The complex physico-chemical properties, in particular its large size and labile nature renders downstream purification of IgM difficult. This review discusses the limitations and challenges associated with the current IgM purification strategies and proposes future directions for research. The uniqueness of affinity chromatography, specifically biomimetic affinity chromatography for protein purification is highlighted and its potential for IgM purification is discussed.
在过去的二十年中，广泛的研究已经使免疫球蛋白-M（IgM）成为一种有潜力的治疗和诊断试剂。为了充分发挥 IgM 的潜力，必须以低成本提供大量高纯度和高活性的 IgM，以进行临床试验、特征研究和定量结构活性分析。其复杂的物理化学性质，特别是其较大的尺寸和不稳定的性质，使得 IgM 的下游纯化变得困难。本文讨论了当前 IgM 纯化策略所面临的限制和挑战，并提出了未来的研究方向。亲和层析的独特性，特别是仿生亲和层析在蛋白质纯化方面的应用，及其在 IgM 纯化方面的应用潜力得到了强调。
