Plasma proteins play many roles in the body and their deficiency leads to many diseases followed by different symptoms where patients require repeated injections of these proteins. In addition, a great number of diagnoses and treatments are based on these proteins (presence and/or quantity). The methods for the fractionation, isolation and purification of proteins from human plasma are of growing need. This need for important quantities of plasma proteins has led researchers to focus their efforts on the development of new methods of fractionation and purification. Chromatographic adsorbents with high affinity, specificity and selectivity were recently developed. The aim of our work is to prepare and examine the separation abilities of a new chromatographic support which is ethylenediamine-diacetic acid polystyrene, to isolate and/or purify human plasmatic proteins using different buffer systems. The purity of the eluent obtained by fractionation of plasma proteins were monitored by SDS-PAGE, which revealed that this resin is able to purify at least two proteins: albumin by MOPS/imidazol buffer (50, 100, and 500 mM). Other proteins are fractionated but not definitively purified ever using different buffer systems (HEPS/EDTA, MOPS/EDTA, with gradient of concentration). In conclusion, the obtained results are promoting and the use of this resin as stationary phase in affinity to prepare sufficient quantities of albumin will be of great utility for treatment of patients suffering from proteins deficiencies like diabetes with albuminurea.