Nearly 60 years ago, Cohen used for the first time using, the plasma fractionation technique, the 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 the Cohen method areis extremely helpful to remove major impurities, before the main building was on the net columns. It works in conjunction with subsequent purification process chromatography could forming a comprehensive process purification of the final product and is of high -purity albumin. Purification was performed on the exchanger anion diethyl amino Sepharose with high speed. It seems that this exchangers, according to agarose structure and cross-linking andwith also a functional area, is used for exchange chromatography column. It appears this exchangers according to agarose lstructure and cross-linking in them, ands also functional extent for use in ion exchange columns which are very suitable. This exchanger has a very weak non-specific adsorption and was not observed to have microbial contamination. With a calculation that was performed on the albumein in the IEC, there is approximately one-third of the initial amount of purification.