Heparinase I Acts on a Synthetic Heparin Pentasaccharide Corresponding to the Antithrombin III Binding Site
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Authors
Yu, Guangli
LeBrun, Laurie
Gunay, Nur Sibel
Hoppensteadt, Debra
Walenga, Jeanine M.
Fareed, Jawed
Linhardt, Robert J.
Issue Date
2000-12-15
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
A synthetic pentasaccharide, containing an intact antithrombin III (ATIII) binding site that is in clinical studies a specific antifactor Xa agent, serves as a substrate for a heparin lyase (heparinase I, EC 4.2.2.7) from Flavobacterium heparinum. Heparinase I, currently being assessed as a heparin reversal agent, also reverses the antifactor Xa activity of this synthetic pentasaccharide by breaking it down to inactive disaccharide and trisaccharide products.
Description
Thrombosis Research, 100, 549-556
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Heparinase I Acts on a Synthetic Heparin Pentasaccharide Corresponding to the Antithrombin III Binding Site, G. Yu, L. LeBrun, N.S. Gunay, D. Hoppensteadt, J. Walenga, J. Fareed, R.J. Linhardt, Thrombosis Research, 100, 549-556, 2000.
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Journal
Volume
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PubMed ID
DOI
ISSN
493848