Selective removal of the autoantibodies from rheumatoid arthritis patient plasma using protein A carrying affinity cryogels

Alkan H., BERELİ N., Baysal Z., DENİZLİ A.

BIOCHEMICAL ENGINEERING JOURNAL, vol.51, no.3, pp.153-159, 2010 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 51 Issue: 3
  • Publication Date: 2010
  • Doi Number: 10.1016/j.bej.2010.06.010
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.153-159
  • Hacettepe University Affiliated: Yes


Rheumatoid arthritis is a chronic, progressive, deabilitating autoimmune disease that occurs in approximately 1% of adults. Rheumatoid arthritis is characterized by chronic polyarthritis and destruction of multiple joints. In this study, IgM-antibody removal from human plasma with supermacroporous poly(hydroxyethyl methacrylate) [PHEMA] cryogel carrying protein A has been evaluated. The PHEMA cryogel was prepared by bulk polymerization which proceeds in an aqueous solution of monomer frozen inside a plastic syringe (cryo-polymerization). After thawing, the PHEMA cryogel contains a continuous matrix having interconnected macropores of 10-200 mu m size. Pore volume in the PHEMA cryogel was 71.6%. Protein A molecules were covalently immobilized onto the PHEMA cryogel via cyanogen bromide (CNBr) activation. The PHEMA cryogel was contacted with blood in in vitro system for the determination of blood-compatibility. The supermacroporous structure of the PHEMA cryogel makes it possible to process blood cells without blocking the cryogel column. IgM-antibody adsorption capacity decreased significantly with the increase of the plasma flow-rate. The maximum IgM-antibody adsorption amount was 42.7 mg/g. IgM-antibody molecules could be repeatedly adsorbed and eluted without noticeable loss in the IgM-antibody adsorption amount. (C) 2010 Elsevier B.V. All rights reserved.