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, immune 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 was 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.