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.
Cite this paper
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