| Literature DB >> 26807703 |
Xuemei Jiang1, Thirumalai Diraviyam1, Xiaoying Zhang2.
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 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.Entities:
Keywords: Affinity purification; Egg yolk immunoglobulin (IgY); Protein M
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Year: 2016 PMID: 26807703 DOI: 10.1016/j.jchromb.2016.01.012
Source DB: PubMed Journal: J Chromatogr B Analyt Technol Biomed Life Sci ISSN: 1570-0232 Impact factor: 3.205