Arakawa Tsutomu
Alliance Protein Laboratories, A Division of KBI Biophama, 6042 Cornerstone Court West, San Diego, CA 92121, United States.
Curr Protein Pept Sci. 2019;20(1):56-60. doi: 10.2174/1389203718666171009111033.
Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.
蛋白质常常会自然地或人为地产生结构异构体，例如，由于不同的糖基化、二硫键重排、部分结构重排、寡聚体形成或化学修饰。异构体的形成通常伴随着电荷状态或疏水性的改变。因此，异构体可以通过反相色谱、疏水相互作用色谱或离子交换色谱进行分离。我们已经应用混合模式色谱对几种模型蛋白的异构体进行分离，并观察到阳离子交换Capto MMC和阴离子交换Capto adhere色谱柱在分离构象异构体和自缔合寡聚体方面是有效的。
