亲和层析
抗体
免疫球蛋白M
化学
计算生物学
免疫球蛋白G
免疫学
生物
生物化学
酶
作者
Satyen Gautam,Kai‐Chee Loh
标识
DOI:10.1016/j.biotechadv.2011.07.001
摘要
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.
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