dc.contributor.author | LeBrun, L.A. | |
dc.contributor.author | Linhardt, Robert J. | |
dc.date | 2001 | |
dc.date.accessioned | 2022-06-27T16:20:26Z | |
dc.date.available | 2022-06-27T16:20:26Z | |
dc.date.issued | 2001-01-01 | |
dc.identifier.citation | Degradation of Heparan Sulfate with Heparin Lyases, L.A. LeBrun, R.J. Linhardt, in Methods in Molecular Biology, Proteoglycan Protocols: Current Methods and Applications, Vol. 171, R.V. Iozzo, ed., Humana Press, Totowa, NJ, Chap. 35, pp 353-361, 2001. | |
dc.identifier.issn | 10643745 | |
dc.identifier.uri | https://doi.org/10.1385/1-59259-209-0:353 | |
dc.identifier.uri | https://hdl.handle.net/20.500.13015/5857 | |
dc.description | in Methods in Molecular Biology, Proteoglycan Protocols: Current Methods and Applications, Vol. 171, R.V. Iozzo, ed., Humana Press, Totowa, NJ, Chap. 35, pp 353-361 | |
dc.description | 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. | |
dc.description.abstract | Glycosaminoglycan (GAG), heparan sulfate (HS), and heparin are a polydisperse mixture of linear polysaccharides composed of glucosamine residues 1→ 4 linked to uronic acid residues. The major repeating unit in heparin is → 4)-α-D-N-sulfoglucosamine-6-sulfate (1? 4)-α-L-iduronic acid-2-sulfate (1?, corresponds to 75-90% of its sequence (1) (see Fig. 1A), whereas heparan sulfate consists of 50-75% ? 4)α-D-N-acetylglucosamine (1? 4)-β-glucuronic acid (1? and smaller amounts of → 4)-α-D-N-acetylglucosamine-6-sulfate (1? 4)-β-D-glucuronic acid (1? and ? 4)α-D-N-sulfoglucosamine (1? 4)-β-D-glucuronic acid (1? (see Fig. 1B). Heparin, which contains approx 2.7 sulfate groups per disaccharide unit, is more highly sulfated than HS, which contains less than one sulfate per disaccharide unit. | |
dc.description.uri | https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1385/1-59259-209-0:353 | |
dc.language | en_US | |
dc.language.iso | ENG | |
dc.relation.ispartof | The Linhardt Research Labs Online Collection | |
dc.relation.ispartof | Rensselaer Polytechnic Institute, Troy, NY | |
dc.relation.ispartof | Methods in molecular biology (Clifton, N.J.) | |
dc.relation.uri | https://harc.rpi.edu/ | |
dc.subject | Biology | |
dc.subject | Chemistry and chemical biology | |
dc.subject | Chemical and biological engineering | |
dc.subject | Biomedical engineering | |
dc.title | Degradation of Heparan Sulfate with Heparin Lyases | |
dc.type | Article | |
dcterms.accessRights | https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1385/1-59259-209-0:353 | |
dcterms.isPartOf | Journal | |
dcterms.isVersionOf | https://doi.org/10.1385/1-59259-209-0:353 | |
dc.rights.holder | In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/ | |
dc.creator.identifier | https://orcid.org/0000-0003-2219-5833 | |
dc.relation.department | The Linhardt Research Labs. | |
dc.relation.department | The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS) | |
rpi.description.pages | 353-361 | |
rpi.description.volume | 171 | |