Hemoglobin Purification Using His-Tag Affinity Chromatography With the Assistance of Ni Ions

In this study, an affinity adsorbent of poly(2-hydroxyethyl methacrylate) [(p(HEMA)] was developed to purify hemoglobin (Hb). Initially, cryogel membranes of p(HEMA) were prepared and their surfaces were modified with the dopamine monomer to create polydopamine (pda) modified p(HEMA) cryogel [pda(HEMA)] membranes. After the modification, the nickel (Ni) ions were immobilized on pda(HEMA ) for Hb purification in the aqueous solution. At pH 5, 23.5 mg/g Hb was adsorbed by the adsorbent and the Langmuir adsorption isotherm model was suitable for this adsorption process thanks to the R2 and q max values; moreover, the prepared adsorbent without notable decreases in its adsorption capacity