Purification of Immunoglobulin Y (IgY) from the Ostrich (Struthio camelus) by Staphylococcal Protein A (SpA) Affinity Chromatography

A. Justiz-Vaillant, P. Akpaka, C. Palmer
Tulane University,
United States

Keywords: immunoglobulin Y (IgY), purification, protein characterization, Staphylococcal protein A (SpA), ostrich


Immunoglobulin Y (IgY) is the major protein present in the avian egg yolk. This antibody fulfils important functions in the protection of Ostrich birds against infections. The aim of this study was to demonstrate the binding capacity of Staphylococcal proteins A (SpA) to Ostrich IgY and assess purification of the IgY by SpA affinity chromatography. Chloroform polyethylene glycol (Polson), affinity chromatography, Enzyme-Linked Immunosorbent Assay (ELISA)and Western blotting methods were used in the process. Results obtained revealed that Ostrich IgY has heavy chain of 70 kDa and light chain of 30 kDa confirming results by Western blot. In addition livetins (egg yolk proteins)were shown in the protein electrophoresis that preceded the Western blot. The binding capacity between SpA and Ostrich IgY is important because SpA can be used as a reagent in immunoassays for antibody detection against microbial agents that usually infect livestocks. This is the first time the use of SpA for purification of Ostrich IgY is being reported in literature.