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Affinity purification of egg yolk immunoglobulins (IgY) using a human mycoplasma protein.

Posted by on in 2016
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2016. J Chromatogr B Analyt Technol Biomed Life Sci. 1012-1013:37-41. doi: 10.1016/j.jchromb.2016.01.012. Epub 2016 Jan 11.

1
College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, China.
2
College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, China. Electronic address: zhang.xy@nwsuaf.edu.cn.

 

 

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.

KEYWORDS:

Affinity purification; Egg yolk immunoglobulin (IgY); Protein M

PMID:
 
26807703
 
DOI:
 
10.1016/j.jchromb.2016.01.012
[Indexed for MEDLINE]
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