Histidine-epoxy-activated sepharose beads embedded poly (2-hydroxyethyl methacrylate) cryogels for pseudobiospecific adsorption of human immunoglobulin G


Corman M. E. , Armutcu C. , BERELİ N. , Elkak A.

JOURNAL OF MACROMOLECULAR SCIENCE PART A-PURE AND APPLIED CHEMISTRY, cilt.54, ss.915-922, 2017 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 54 Konu: 12
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1080/10601325.2017.1381921
  • Dergi Adı: JOURNAL OF MACROMOLECULAR SCIENCE PART A-PURE AND APPLIED CHEMISTRY
  • Sayfa Sayıları: ss.915-922

Özet

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 degrees C and pH 7.4 and was found to be 26.95mg/g of cryogel which is close to that obtained experimentally (24.49mg/g). The cryogels were used for several adsorption-desorption cycles without any negligible decrease in their adsorption capacity.