Volume 41 - Issue 3 - 279 - 288

Depletion of Albumin From Human Serum by Monosize Affinity Beads

Eş boyutlu manyetik affinite partiküller ile insan serumundan albumin uzaklaştırılması

The hydrophobic affinity ligand L-tryptophan immobilized magnetic poly(glycidyl methacrylate) [m-poly(GMA)] beads in monosize form (1.6μm in diameter) were used for the affinity depletion of human serum albumin [HSA]. The m-poly(GMA) beads were prepared by dispersion polymerization in the presence of Fe3O4 nano-powder. The epoxy groups of the m-poly(GMA) beads were converted into amino groups by using 1,6 diaminohexane (i.e., spacer arm). L-tryptophan was then covalently immobilized on spacer arm attached m-poly(GMA) beads. Elemental analysis of immobilised L-tryptophan for nitrogen was estimated as 42.5 μmol/g polymer. Adsorption studies were performed under different conditions in a batch system (i.e., medium pH, protein concentration and temperature). Maximum lysozyme adsorption amount of m-poly(GMA) and L-tryptophan immobilized m-poly(GMA) [m-poly(GMA)-L-tryptophan] beads were 1.78 and 172.9 mg/g, respectively. The applicability of two kinetic models including pseudo-first order and pseudo-second order model was estimated. It was also observed that after 5 adsorption–elution cycle, m-poly(GMA)-L-tryptophan beads can be used without significant loss in HSA adsorption capacity. The elution results demonstrated that the adsorption of HSA to the adsorbent was reversible. 

Download Article in PDF (635 kB)

  • ISSN 1303 5002
  • © 1973-2019 Hacettepe University