HCl). Batch adsorption studies were performed in order to evaluate the effect of buffer pH and nature on IgG uptake as well the equilibrium isotherms. Chromatographic experiments were performed with both human IgG (high purity) and human serum and each buffer with NaCl 1.0?M was used in the elution step. Best results (maximum equilibrium adsorption capacity of 110.9?mg?g?) were found at pH 7.8 with Tris-a href='/search?dc.title=HCl&facet-content-type=ReferenceWorkEntry&sortOrder=relevance' class='reference-link webtrekk-track' gaCategory="Internal link" gaLabel="HCl" gaAction="reference keyword">HCl buffer. The Langmuir–Freundlich model provided a good fit for the adsorption isotherm. In chromatographic experiments with high purity IgG and Tris/HCl buffer, IgG dynamic adsorption capacity onto E-Ch/Al-Cibacron was 13.4?mg?g?, which accounted for 60?% of IgG injected into the column. Chromatographic experiments with diluted (tenfold) human serum were conducted and it was found by electrophoresis that IgG is preferentially adsorbed with respect to other proteins using all buffers systems, especially with Tris-a href='/search?dc.title=HCl&facet-content-type=ReferenceWorkEntry&sortOrder=relevance' class='reference-link webtrekk-track' gaCategory="Internal link" gaLabel="HCl" gaAction="reference keyword">HCl. The amount of desorbed protein from E-Ch/Al-Cibacron was around 7.0?mg?g? for all buffers. The new stationary phase showed high affinity for IgG and may be a potential adsorbent for human IgG purification." />