Author/Authors :
IJour-Amir, M Dept - of Biochemistry - Bobo! Univ, of Med. Sciences , Rasaee, M.J Dept - of Biochemistty - Tarbiat-Modares Univ, Tehran , Qujeq, D Dept - of Biochemistry - Bobo! Univ, of Med. Sciences , Asadikaram, GIIR Dept - of Biochemistty - Rafsanjan Univ, of Med. Sciences , Frozandeh Moqhadam, M Dept - of Biochemistty - Tarbiat-Modares Univ, Tehran
Abstract :
The use of immunoglobulin Y (IgY) instead of polyclonal antibodies prepared in mammals has been reported recently. These antibodies are found to have better properties in terms of specificity and ease of large scale production. In this study, proteins from egg yolk were extracted with acid and chloroform. The result of cellulose acetate electrophoresis at pH 9 showed some extra bands which were further purified with sodium sulfate precipitation (20%). The purified band was observed in the y globulin region. SDS-PAGE eletrophoresis of the product showed impurities which were removed by T-gel chromatography. Following that only H-chain-of immunoglobulin Y with a molecular weight of about 66 KD was observed. Using the above procedure, a yield of around 40.7 mg IgY / egg was obtained.
