Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7616431 | Journal of Chromatography B | 2016 | 18 Pages |
Abstract
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 IgYÎFc, based on pull down and western blot investigations; in addition, it was found that â¼125 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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Xuemei Jiang, Thirumalai Diraviyam, Xiaoying Zhang,