Egg white is one of the important nutrients that frequently induces
   allergic reactions, particulary in atopic children .The proteins of egg white
   are common causes of hyper - sensitivity  symptoms among atopic
   individuals so in the way of studying the allergy to egg , it is essential to purify
   egg white proteins .

          In the present study , ion exchange chromatography , immuno
   electrophoresis (IE) and  polyacrylamid gel electrophoresis  (SDS-PAGE )
   were used  for separation  and  purification of egg white proteins .

          Following ion exchange chromatography, three fractions including : F1,
   F2,F3 were distinguished and isolated in concrete pHs . The isolated fractions
   were analysed by SDS - PAGE and  IE . The results indicated several  protein
   bands in F1 , a single protein  band in   F2  and  a  major  protein  band 
   with  minor  impurity  in  F3 .  Also  molecular weight  of  the isolated fractions 
   were determined by SDS-PAGE, so F2 and F3 identified as ovotransferrin
   (conalbumin ) and ovalbumin respectively .

          The study indicated that ovotransferrin was highly pure , whereas 
   ovalbumin included a little impurity .