Author(s)

Mrigendra Rajput^1*, Shimaa M. G. Mansour², Lyle J. Braun³, Mahmoud Darweesh³, Neelu Thakur³, Christopher C. L. Chase³

¹Medgene Labs, Brookings, SD, USA.
²Department of Virology, Faculty of Veterinary Medicine, Zagazig University, Zagazig, Egypt.
³Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD, USA.

The purified Immunoglobulin G (IgG) is effectively used in passive immunization. There are various methods to isolate the IgG from serum, with its own advantages and disadvantages. In the current study, a comparative efficacy of the affinity chromatography using Protein A—Sepharose and ion exchange chromatography using DEAE Sephadex A50 was done with regard to yield and purity of IgG. Both methods were found equally effective in isolation of pure IgG with similar recovery, indicating that researcher can use either method to purify IgG depending on available resources.

Affinity Chromatography, Ion Exchange Chromatography, Bovine Immunoglobin G

Rajput, M., Mansour, S.M.G., Braun, L.J., Darweesh, M., Thakur, N. and Chase, C.C.L. (2014) Comparison of the Affinity Chromatography and the Ion Exchange Chromatography in the Isolation of Bovine Immunoglobin G. Open Access Library Journal, 1, 1-5. doi: 10.4236/oalib.1100960.