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

Year 2024, Volume: 52 Issue: 4, 243 - 252, 11.10.2024

Muhammed Erkek , Merve Çalışır , Aykut Arif Topçu , Adil Denizli

https://doi.org/10.15671/hjbc.1454485

Abstract

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

Keywords

hemoglobin, adsorption, affinity chromatography, his-tag affinity chromatography, cryogel.

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