Kiraly, J., Vareckova, E., Mucha, V. and Kostolansky, F. (2011) Evaluation of Anti-Influenza Efficiency of Polyclonal IgG Antibodies Specific to the Ectodomain of M2 Protein of Influenza A Virus by Passive Immunization of Mice. Acta Virologica, 55, 261-265.
http://dx.doi.org/10.4149/av_2011_03_261

has been cited by the following article:

• TITLE: Comparison of the Affinity Chromatography and the Ion Exchange Chromatography in the Isolation of Bovine Immunoglobin G

  AUTHORS: Mrigendra Rajput, Shimaa M. G. Mansour, Lyle J. Braun, Mahmoud Darweesh, Neelu Thakur, Christopher C. L. Chase

  KEYWORDS: Affinity Chromatography, Ion Exchange Chromatography, Bovine Immunoglobin G

  JOURNAL NAME: Open Access Library Journal, Vol.1 No.6, September 18, 2014

  ABSTRACT: 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.