Affinity capillary electrophoresis for the determination of binding affinities for low molecular weight heparins and antithrombin-III

Dinges M. M., Solakyıldırım K., Larive C. K.

Electrophoresis, vol.35, no.10, pp.1469-1477, 2014 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 35 Issue: 10
  • Publication Date: 2014
  • Doi Number: 10.1002/elps.201300549
  • Journal Name: Electrophoresis
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1469-1477
  • Keywords: ACE, Dalteparin, Enoxaparin, Fondaparinux, Tinzaparin
  • Erzincan Binali Yildirim University Affiliated: No


The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa. The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue. ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Determination of the AT-III binding affinities of the LWMHs is complicated by their inherent structural heterogeneity and polydispersity. The fractional composition of 3-O-sulfo-N-sulfoglucosamine residues was determined for each drug substance using 2D NMR and used in the interpretation of the ACE results. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.