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Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
Purification of immunoglobulins using protein a-sepharose
1Biochemistry Department, Rothamsted Experimental Station, Hertfordshire, UK.
Most immunochemical techniques used in molecular biology rely on a specific class of antibodies, immunoglobulin G (IgG). In mammals, IgG antibodies are produced during the secondary humoral response and contribute about 80% of the serum immunoglobulin. Factors affecting the experimental production of antibodies have been discussed in detail (1). In this chapter we describe a method for the rapid and efficient purification of IgG to near homogeneity from rabbit serum. This is achieved by affinity chromatography using protein A.
Most immunochemical techniques used in molecular biology rely on a specific class of antibodies, immunoglobulin G (IgG). In mammals, IgG antibodies are produced during the secondary humoral response and contribute about 80% of the serum immunoglobulin. Factors affecting the experimental production of antibodies have been discussed in detail (1). In this chapter we describe a method for the rapid and efficient purification of IgG to near homogeneity from rabbit serum. This is achieved by affinity chromatography using protein A.

