Abstract
Multifunctional polymer-derivatized superparamagnetic iron oxide (γ-Fe 2O 3) nanoparticles were prepared for biomagnetic separation of histidine-tagged recombinant proteins building up a faster and efficient method for protein separation by making use of their intrinsic magnetic properties. Using polymer bound γ-Fe 2O 3 nanocrystals, a 6× histidine-tagged recombinant protein (silicatein) with a molecular weight of 24 kDa has been isolated and purified. The supermagnetic iron oxide nanocrystals were characterized by transmission electron microscopy (TEM), high-resolution TEM (HRTEM), SQUID and Mössbauer and the polymer functionalization of the γ-Fe 2O 3 nanocrystals was monitored by UV–vis spectroscopy and light microscopy. Protein immobilization and separation was monitored using immunostaining techniques and gel electrophoresis, respectively.
Published Version
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