Nearly 60 years ago, Cohen, for the first time was using the plasma fractionation technique, plasma protein purification method developed for large-scale production. Cohen and colleagues, in the mid-20th century, took the first steps in the field of plasma fractionation technology. In the present study, albumin first was purified with the Cohen method, and thereupon it was purified, using ion exchange chromatography on DEAE Sepharose gel. It should be noted that the initial human serum albumin purification through precipitation with Cohen method are extremely helpful to remove major impurities, before the main building was on the net columns. It works in conjunction with a subsequent purification process chromatography could form a comprehensive process purification of the final product is of high purity albumin. Purification was performed on the exchanger anion diethyl amino Sepharose with high speed. It seems that thiese exchangers, according to agarose structure and cross-linking, and also functional area is used for exchange chromatography column. It appears thisat exchangers, according to agarose structure and cross-linking in them, and also functional extent for use in ion exchange columns are very suitable. This exchanger has a very weak non-specific adsorption, and wasith not observed microbial contamination. With a calculation that was performed on the albumen in the IEC, approximately one-third of the initial amount of purification was used.