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Nonspecific Electrostatic Binding Characteristics of the Heparin-antithrombin Interaction by Emek Seyrek; Paul L. Dubin; Jens Henriksen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract We evaluated the role of nonspecific electrostatic binding in the interaction of antithrombin (AT) with heparin (Hp), a paradigmatic protein‐glycosaminoglycan (GAG) system. To do so, we obtained the ionic‐strength dependence of the binding constant, since a common feature in protein‐polyelectrolyte systems is a maximum in affinity in the ionic strength range 10 m__M__ <__I__<30 m__M__ (Seyrek et al, Biomacromolecules 2003, 4, 273‐282). Because this feature is seen for both synthetic and biological polyelectrolytes, and because the value of __I__~max~ correlates with protein size and charge asymmetry through the Debye length (Seyrek et al, Biomacromolecules 2003, 4, 273‐282), this behavior appears to be a signature of non‐specific electrostatic protein‐polyelectrolyte binding. Binding of AT to both standard (14 kDa) Hp and partially degraded (5 kDa) low molecular weight heparin (LMWH) exhibited this same behavior. Capillary electrophoresis (CZE) of Hp and LMWH yielded electropherograms whose remarkable breadth revealed the enormous heterogeneity of average charge density among the innumerable molecular species of Hp and LMWH. These distributions were somewhat reduced aft

Who reads Nonspecific Electrostatic Binding Characteristics of the Heparin-antithrombin Interaction?

Author

Emek Seyrek; Paul L. Dubin; Jens Henriksen

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)