Histidine-epoxy-activated sepharose beads embedded poly (2-hydroxyethyl methacrylate) cryogels for pseudobiospecific adsorption of human immunoglobulin G. Issue 12 (2nd December 2017)

• Record Type: Journal Article
• Authors: Çorman, Mehmet Emin; Armutcu, Canan; Bereli, Nilay; Elkak, Assem
• Is Part Of: Journal of macromolecular science. Volume 54:Issue 12(2017)
• Page Start: 915
• Page End: 922
• Publication Date: 2017-12-02
• Subjects: histidine-sepharose -- pHEMA -- cryogels -- pseudobioaffinity -- human IgG; Polymers -- Periodicals; Polymerization -- Periodicals; 547.7
• DOI: 10.1080/10601325.2017.1381921
• Languages: English
• ISSNs: 1060-1325

Abstract

ABSTRACT: The use of highly purified immunoglobulin became among the most powerful adopted strategies in therapeutic trials nowadays. Their role as immunomodulatory and anti-inflammatory agents has widened their scope of use. A novel continuous supermacroporous monolithic cryogels embedded with histidine-epoxy-activated-sepharose beads were synthetized as a new monolithic adsorbents for the separation of immunoglobulin G from human serum. The histidine-epoxy-activated-sepharose beads were embedded into the 2-hydroxyethyl methacrylate (HEMA) cryogels present in frozen aqueous solution inside a plastic syringe. The microstructure morphology of the cryogels was characterized by swelling measurement and scanning electron microscopy. The adsorption of human IgG on the histidine-epoxy-activated-sepharose beads pHEMA cryogels appeared to follow the Langmuir–Freundlich adsorption isotherm model. The maximum IgG adsorption was observed at 4°C and pH 7.4 and was found to be 26.95 mg/g of cryogel which is close to that obtained experimentally (24.49 mg/g). The cryogels were used for several adsorption-desorption cycles without any negligible decrease in their adsorption capacity.