Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography.
Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography.
复制标题
DOI：
10.1016/j.chroma.2008.12.004
复制
发表时间：
2009-02
期刊：
影响因子：
--
通讯作者：
Haiou Yang;P. V. Gurgel;R. Carbonell
中科院分区：
文献类型：
--
作者：
Haiou Yang;P. V. Gurgel;R. Carbonell
线性Fc结合六聚体肽家族（HWRGWV、HYFKFD和HFRRHL）的色谱树脂表现出从完全哺乳动物细胞培养基（cMEM）中选择性吸附和分离人IgG（hIgG）的能力。其中，肽密度为0.08mequiv./ g树脂能够以高达95%的纯度和产率从cMEM中纯化hIgG，与蛋白A和A2 P琼脂糖凝胶相当。还研究了HWRGWV树脂的N-末端乙酰化、树脂上的配体密度、初始hIgG浓度和温度对IgG分离的影响。结果表明，这些小肽配体，特别是HWRGWV，提供了一个潜在的替代使用蛋白A或蛋白G的大规模亲和色谱。
Chromatographic resins of a family of linear Fc-binding hexamer peptides (HWRGWV, HYFKFD, and HFRRHL) exhibited the ability to selectively adsorb and isolate human IgG (hIgG) from complete mammalian cell culture medium (cMEM). Among them, the HWRGWV resin with a peptide density of 0.08mequiv./g of resin was able to purify hIgG from cMEM with both purity and yield as high as 95%, comparable to Protein A and A2P agarose gels. The influences of N-terminal acetylation of the HWRGWV resin, ligand density on the resin, initial hIgG concentration, and temperature on IgG isolation were also investigated. The results indicate that these small peptide ligands, especially HWRGWV, offer a potential alternative to the use of Protein A or Protein G for large scale affinity chromatography.