Enzymatic Modification of Heparan Sulfate on a Biochip Promotes Its Interaction with Antithrombin III

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Authors
Hernaiz, Maria
Liu, Jian
Rosenberg, Robert D.
Linhardt, Robert J.
Issue Date
2000-09-16
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Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
A heparan sulfate glycosaminoglycan chain, biotinylated at its reducing-end, was bound to a streptavidin-coated biochip. Surface plasmon resonance spectroscopy showed a low affinity interaction with antithrombin III (ATIII) when it was flowed over a surface containing heparan sulfate. ATIII bound tightly with high affinity when the same surface was enzymatically modified to using 3-O-sulfotransferase isoform 1 (3-OST-1) in the presence of 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. This experiment demonstrates the specific structural modification of a glycosaminoglycan bound to a biochip using a biosynthetic enzyme, suggesting a new approach to rapid screening glycosaminoglycan-protein interactions.
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Biochemical Biophysical Research Communications, 276, 292-297
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Full Citation
Enzymatic Modification of Heparan Sulfate on a Biochip Promotes Its Interaction with Antithrombin III, M. Hernaiz, J. Liu, R.D. Rosenberg, R.J. Linhardt, Biochemical Biophysical Research Communications, 276, 292-297, 2000.
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0006291X
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