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A Method for the Non-covalent Immobilization of Heparin to Surfaces by David J Mahoney; Jason D Whittle; Caroline M Milner; Simon J Clark; Barbara Mulloy; David J Buttle; Gavin C Jones; Anthony J Day; Robert D Short is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is A Method for the Non-covalent Immobilization of Heparin to Surfaces about?

The interaction of heparan sulfate (HS) with speciWc proteins facilitates a wide range of fundamental biological processes including cellular proliferation and diVerentiation, tissue homeostasis, and viral pathogenesis. This multiplicity of function arises through sequence diversity within the HS chain. Heparin, which is very similar in structure to the sulfated regions of HS, is an excellent model for studying HS-protein interactions. The development of high-throughput enzyme-linked immunosorbent-like assays using surfaceimmobilized heparin has been hindered by the inability of this glycosaminoglycan to adhere to microtiter surfaces. Here we report the passive noncovalent adsorption of heparin onto microtiter wells following their treatment by plasma polymerization; there was no detectable binding of functional heparin onto untreated plates. Heparin immobilized in this way was able to interact with four diVerent heparin-binding proteins tested, i.e., TSG-6, chemokines IL-8 and KC, and complement factor H. Heparin preparations ranging in size from high molecular weight to a deWned decasaccharide could be adsorbed onto these plates in a functionally active form. Since plasma polymer

Who reads A Method for the Non-covalent Immobilization of Heparin to Surfaces?

Author

David J Mahoney; Jason D Whittle; Caroline M Milner; Simon J Clark; Barbara Mulloy; David J Buttle; Gavin C Jones; Anthony J Day; Robert D Short

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)