Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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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.
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 220.127.116.11) 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.;
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.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Thrombosis Research; https://harc.rpi.edu/;