Serum proteins are the most abundant compounds in human serum. Abnormal synthesis or elimination of one or more of these proteins can lead to deficits and many symptomatic conditions. The administration of the relevant protein(s) is the only way of the treatment. The aim of the present study was to fractionate blood plasma proteins and to provide health professional drugs. In this context, a method of immobilized metal affinity chromatography chelate (IMAC) is developed using of polystyrene suported acetylacetone-di(3-aminopropyl) amine Schiff base as a chelating resin of divalent metal ions. The purification and depletion of plasma proteins in human serum was studied. The purity of the obtained eluents of chromatographic fractionation of plasma proteins was monitored by SDS-PAGE. Results indicated that the resin-Cu used as stationary phase was able to purify the albumin when Trist-HCl 100mM, pH7 was the mobile phase. In conclusion, the results of the present study can be considered as a starting point for the development of a new technique to purify human serum albumin that can be used in scientific research, diagnosis and treatment.