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dc.contributor.authorIslam, Tasneem
dc.contributor.authorButler, Melissa
dc.contributor.authorSikkander, Sulthan A.
dc.contributor.authorToida, Toshihiko
dc.contributor.authorLinhardt, Robert J.
dc.date.accessioned2006-08-06
dc.date.accessioned2015-04-29T23:47:00Z
dc.date.accessioned2017-03-02T01:08:37Z
dc.date.available2015-04-29T23:47:00Z
dc.date.available2017-03-02T01:08:37Z
dc.date.issued2002
dc.identifier.issn0008-6215
dc.identifier.doi10.1016/S0008-6215(02)00229-X
dc.identifier.urihttp://hdl.handle.net/10072/67448
dc.description.abstractPorcine mucosal heparin was fragmented into low-mol.-wt. (LMW) heparin by treatment of periodate-oxidized heparin with sodium hydroxide, followed by redn. with sodium borohydride and acid hydrolysis. Gradient polyacrylamide gel electrophoresis anal. showed a mixt. of heparin fragments with an av. size of eight disaccharide units. 1D 1H NMR showed two-thirds of the N-acetyl groups were lost on periodate cleavage, suggesting cleavage had occurred at the glucopyranosyluronic acid (GlcpA) and idopyranosyluronic acid (IdopA) residues located within and adjacent to the antithrombin III (ATIII) binding site. The N-acetyl glucopyranose (GlcpNAc) residue was lost on workup. The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo,3,6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue. Thus, periodate cleaved heparin should be enriched in GlcpNS3S6S residues. Two-dimensional correlation spectroscopy (2D COSY) confirmed that LMW heparin prepd. through periodate cleavage contained GlcpNS3S6S at its non-reducing end. As expected, this LMW heparin also showed reduced ATIII mediated anti-factor IIa and anti-factor Xa activities.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.publisherElsevier Science
dc.publisher.placeU.S.A
dc.relation.ispartofpagefrom2239
dc.relation.ispartofpageto2243
dc.relation.ispartofissue21-23
dc.relation.ispartofjournalCarbohydrate Research
dc.relation.ispartofvolume337
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchOrganic Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0305
dc.subject.fieldofresearchcode0601
dc.titleFurther evidence that periodate cleavage of heparin occurs primarily through the antithrombin binding site
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codec1x
gro.facultyInstitute for Glycomics
gro.hasfulltextNo Full Text
gro.griffith.authorIslam, Tasneem


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