AuthorXiao, Zhongping; Tappen, Britney R.; Ly, Mellisa; Zhao, Wenjing; Canova, Lauren P.; Guan, Huashi; Linhardt, Robert J.
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationHeparin mapping using heparin lyases and the generation of a novel low molecular weight heparin, Z. Xiao, B. R. Tappen, M. Ly, W. Zhao, L. P. Canova, H. Guan, R. J. Linhardt, Journal of Medicinal Chemistry, 54, 603–610, 2011. 2011.
AbstractSeven pharmaceutical heparins were investigated by oligosaccharide mapping by digestion with heparin lyase 1, 2, or 3, followed by high performance liquid chromatography analysis. The structure of one of the prepared mapping standards, ΔUA-Gal-Gal-Xyl-O-CH(2)CONHCH(2)COOH (where ΔUA is 4-deoxy-α-l-threo-hex-4-eno-pyranosyluronic acid, Gal is β-d-galactpyranose, and Xyl is β-d-xylopyranose) released from the linkage region using either heparin lyase 2 or heparin lyase 3 digestion, is reported for the first time. A size-dependent susceptibility of site cleaved by heparin lyase 3 was also observed. Heparin lyase 3 acts on the undersulfated domains of the heparin chain and does not cleave the linkages within heparin's antithrombin III binding site. Thus, a novel low molecular weight heparin (LMWH) is afforded on heparin lyase 3 digestion of heparin due to this unique substrate specificity, which has anticoagulant activity comparable to that of currently available LMWH.;
DescriptionJournal of Medicinal Chemistry, 54, 603–610; 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.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
PublisherAmerican Chemical Society (ACS)
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Medicinal Chemistry; https://harc.rpi.edu/;
AccessA full text version is available in DSpace@RPI;