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dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorTurnbull, J.E.
dc.contributor.authorWang, H.M.
dc.contributor.authorLoganathan, D.
dc.contributor.authorGallagher, J.T.
dc.date1990
dc.date.accessioned2022-06-27T17:15:22Z
dc.date.available2022-06-27T17:15:22Z
dc.date.issued1990-03-01
dc.identifier.citationExamination of the Substrate Specificity of Heparin and Heparan Sulfate Lyases, R.J. Linhardt, J.E. Turnbull, H.M. Wang, D. Loganathan, J.T. Gallagher, Biochemistry, 29, 2611-2617 (1990).
dc.identifier.issn15204995
dc.identifier.issn62960
dc.identifier.urihttps://doi.org/10.1021/bi00462a026
dc.identifier.urihttps://hdl.handle.net/20.500.13015/6007
dc.descriptionBiochemistry, 29, 2611-2617
dc.descriptionNote : 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.abstractWe have examined the activities of different preparations of heparin and heparan sulfate lyases from Flavobacterium heparinum. The enzymes were incubated with oligosaccharides of known size and sequence and with complex polysaccharide substrates, and the resulting degradation products were analyzed by strong-anion-exchange high-performance liquid chromatography and by oligosaccharide mapping using gradient polyacrylamide gel electrophoresis. Heparinase (EC 4.2.2.7) purified in our laboratory and a so-called Heparinase I (Hep I) from a commercial source yielded similar oligosaccharide maps with heparin substrates and displayed specificity for di- or trisulfated disaccharides of the structure----4)-alpha-D-GlcNp2S(6R)(1----4)-alpha-L-IdoAp2S( 1----(where R = O-sulfo or OH). Oligosaccharide mapping with two different commercial preparations of heparan sulfate lyase [heparitinase (EC 4.2.2.8)] indicated close similarities in their depolymerization of heparan sulfate. Furthermore, these enzymes only degraded defined oligosaccharides at hexosaminidic linkages with glucuronic acid:----4)-alpha-D-GlcNpR(1----4)-beta-D-GlcAp(1----(where R = N-acetamido or N-sulfo). The enzymes showed activity against solitary glucuronate-containing disaccharides in otherwise highly sulfated domains including the saccharide sequence that contains the antithrombin binding region in heparin. A different commercial enzyme, Heparinase II (Hep II), displayed a broad spectrum of activity against polysaccharide and oligosaccharide substrates, but mapping data indicated that it was a separate enzyme rather than a mixture of heparinase and heparitinase/Hep III. When used in conjunction with the described separation procedures, these enzymes are powerful reagents for the structural/sequence analysis of heparin and heparan sulfate.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi00462a026
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleExamination of the Substrate Specificity of Heparin and Heparan Sulfate Lyases
dc.typeArticle
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dcterms.isVersionOfhttps://doi.org/10.1021/bi00462a026
dc.rights.holderIn 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.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages2611-2617
rpi.description.volume29


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