Affinity capillary electrophoresis for the determination of binding affinities for low molecular weight heparins and antithrombin-III.
Electrophoresis
; 35(10): 1469-77, 2014 May.
Article
em En
| MEDLINE
| ID: mdl-24616065
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Antitrombina III
/
Heparina de Baixo Peso Molecular
/
Eletroforese Capilar
Idioma:
En
Revista:
Electrophoresis
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos