File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1093/glycob/9.12.1331
- Scopus: eid_2-s2.0-0033456287
- PMID: 10561458
- WOS: WOS:000084044200006
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: A novel strategy to generate biologically active neo-glycosaminoglycan conjugates
Title | A novel strategy to generate biologically active neo-glycosaminoglycan conjugates |
---|---|
Authors | |
Keywords | Antithrombin Heparin Neo-glycosaminoglycan Thrombin |
Issue Date | 1999 |
Publisher | Oxford University Press. The Journal's web site is located at http://glycob.oxfordjournals.org/ |
Citation | Glycobiology, 1999, v. 9 n. 12, p. 1331-1336 How to Cite? |
Abstract | Heparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin. |
Persistent Identifier | http://hdl.handle.net/10722/179405 |
ISSN | 2023 Impact Factor: 3.4 2023 SCImago Journal Rankings: 1.045 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Rong, J | en_US |
dc.contributor.author | Nordling, K | en_US |
dc.contributor.author | Björk, I | en_US |
dc.contributor.author | Lindahl, U | en_US |
dc.date.accessioned | 2012-12-19T09:56:13Z | - |
dc.date.available | 2012-12-19T09:56:13Z | - |
dc.date.issued | 1999 | en_US |
dc.identifier.citation | Glycobiology, 1999, v. 9 n. 12, p. 1331-1336 | en_US |
dc.identifier.issn | 0959-6658 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179405 | - |
dc.description.abstract | Heparin and heparan sulfate are structurally related polysaccharides with a variety of biological effects/functions. Most of these effects are due to interactions, of varying specificity, between the negatively charged polysaccharide chains and proteins. While such interactions generally involve a single saccharide domain of decasaccharide size or less, ternary complexes of two protein molecules binding to separate domains on a single polysaccharide chain are known to occur. To facilitate studies on domain organization and its importance for biological function a strategy was developed to chemically conjugate defined heparin oligomers in linear and chemoselective fashion. The procedure requires that the oligosaccharide to provide the reducing-terminal domain of the conjugate is generated by lyase degradation of a parent polysaccharide, whereas the nonreducing-terminal domain is obtained through deaminative cleavage with nitrous acid. The applicability of the method was demonstrated by constructing a conjugate composed of two heparin 12-mers, of which the reducing-terminal component contained the antithrombin-binding region, whereas the nonreducing-terminal domain did not. Contrary to any of the unconjugated oligomers, the product was found to efficiently promote the inactivation of thrombin by antithrombin. | en_US |
dc.language | eng | en_US |
dc.publisher | Oxford University Press. The Journal's web site is located at http://glycob.oxfordjournals.org/ | en_US |
dc.relation.ispartof | Glycobiology | en_US |
dc.subject | Antithrombin | - |
dc.subject | Heparin | - |
dc.subject | Neo-glycosaminoglycan | - |
dc.subject | Thrombin | - |
dc.subject.mesh | Anticoagulants - Pharmacology | en_US |
dc.subject.mesh | Antithrombins - Chemistry - Pharmacology | en_US |
dc.subject.mesh | Chromatography, Gel | en_US |
dc.subject.mesh | Glycosaminoglycans - Chemistry - Pharmacology | en_US |
dc.subject.mesh | Heparin - Chemistry - Pharmacology | en_US |
dc.subject.mesh | Molecular Structure | en_US |
dc.subject.mesh | Oligosaccharides - Chemistry | en_US |
dc.subject.mesh | Osmolar Concentration | en_US |
dc.subject.mesh | Thrombin - Antagonists & Inhibitors | en_US |
dc.title | A novel strategy to generate biologically active neo-glycosaminoglycan conjugates | en_US |
dc.type | Article | en_US |
dc.identifier.email | Rong, J: jrong@hku.hk | en_US |
dc.identifier.authority | Rong, J=rp00515 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1093/glycob/9.12.1331 | - |
dc.identifier.pmid | 10561458 | - |
dc.identifier.scopus | eid_2-s2.0-0033456287 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0033456287&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 9 | en_US |
dc.identifier.issue | 12 | en_US |
dc.identifier.spage | 1331 | en_US |
dc.identifier.epage | 1336 | en_US |
dc.identifier.isi | WOS:000084044200006 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Rong, J=7005980047 | en_US |
dc.identifier.scopusauthorid | Nordling, K=6603000615 | en_US |
dc.identifier.scopusauthorid | Björk, I=7005841773 | en_US |
dc.identifier.scopusauthorid | Lindahl, U=35473807100 | en_US |
dc.identifier.issnl | 0959-6658 | - |