化学
亲和层析
抗体
色谱法
蛋白质纯化
串联亲和纯化
蛋白质A
免疫印迹
单克隆抗体
蛋黄
蛋白质G
分子生物学
生物化学
生物
酶
免疫学
基因
食品科学
作者
Xin Jiang,Thirumalai Diraviyam,Xiaoying Zhang
标识
DOI:10.1016/j.jchromb.2016.01.012
摘要
Egg yolk immunoglobulin (IgY) is a superior functional equivalent to mammalian IgG. However, the preparation of refined and highly purified IgY is still attributed as difficult task. Protein M (a transmembrane protein from human mycoplasma) has been newly demonstrated as an ideal affinity regent for mammalian antibody purification. This study aimed to evaluate the interaction between protein M and IgY. The results showed protein M could be a superior affinity reagent for IgY, scFv as well as IgYΔFc, based on pull down and western blot investigations; in addition, it was found that ∼125 times increase of effective IgY in the elutent was obtained using protein M affinity chromatography column compared with traditional IgY extraction methods. This indicates, the purification strategy of protein M is entirely different to traditional IBPs and the salient purification feature of protein M would be a breakthrough for purifying not only non-mammalian antibodies, but also monoclonal antibodies and engineered antibodies based on variable region.
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