The present work intended to introduce an innovative experimental protocol aiming at improving the well known difficult purification process of heparin (HEP) from other glycosaminoglycans. This strategy lied in the idea of synthesizing the HEP/heparan sulfate (HS) interacting protein fragment (RPKAKAKAKAKDQTK) denoted HIP [1] and assembled deliberately in a commercial anion exchanger resin (DEAE-MacroPrep^®). This acrylamide-type polymer is characterized by having much higher exclusion limit than the resins used routinely for peptide synthesis. The uncommon use of this type of commercial resin for peptide synthesis was previously verified by our group [2,3] and the present approach might enable this HIP-resin to be used as a combined anion exchange - affinity chromatography for the challenging fractionation of HEP and fragments. Besides HEP, HS, chondroitin and dermatan sulfates  (CS and DS, respectively) were selected for the purification experiments using also the peptide-free DEAE-MacroPrep^®) for comparison. The salt-gradient ranging from 0 to 2 M NaCl was applied in the chromatographic procedure with solutes detection and characterization carried out as previously described [4,5]. The results herein collected allowed the following conclusions: i) CS followed by DS are faster eluted in both peptide-free and HIP-resin, showing a good separation between them; ii) otherwise, the retention of HS and HEP was clearly higher in the HIP-support than in DEAE-MacroPrep^®; iii) in addition, an improved separation between these components was also verified with the former resin; iv) lastly, only the HIP-resin depicted partial fractionation of the components of the HEP used in these experiments. Hence, these findings indicated clearly the importance of the affinity effect induced by the peptide segment attached to the polymer and that, for the first time, an unusual but valuable chromatographic approach seemed to be introduced for help fractionate more successfully some type of carbohydrates. Further variation in the chromatographic protocol such as the increase in the size of column or in the gradient applied might result in higher yield of purification. [1] Arteriosclerosis (1989) 9, 21; [2] Anal. Biochem. (2003) 318, 39; [3] J. Chromatography B (2005) 817, 231; [4] J. Biol. Chem. (1990) 265, 16807; [5] J. Biol. Chem. (2002) 277, 48227. Supported by FAPESP, Capes and CNPq.