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dc.contributor.authorZhang, Zhenqing
dc.contributor.authorPark, Youmie
dc.contributor.authorKemp, Melissa M.
dc.contributor.authorZhao, Wenjing
dc.contributor.authorIm, A. Rang
dc.contributor.authorShaya, David
dc.contributor.authorCygler, Miroslaw
dc.contributor.authorKim, Yeong Shik
dc.contributor.authorLinhardt, Robert J.
dc.date2008
dc.date.accessioned2022-06-27T16:11:45Z
dc.date.available2022-06-27T16:11:45Z
dc.date.issued2009-02-01
dc.identifier.citationLiquid Chromatography-Mass Spectrometry to Study Chondroitin Lyase Action Pattern, Z. Zhang, Y. Park, M. M. Kemp, W. Zhao, A.-R. Im, D. Shaya, M. Cygler, Y. S. Kim, R. J. Linhardt, Analytical Biochemistry, 385, 57-64, 2008.
dc.identifier.issn10960309
dc.identifier.issn32697
dc.identifier.urihttps://doi.org/10.1016/j.ab.2008.10.014
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5756
dc.descriptionAnalytical Biochemistry, 385, 57-64
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.abstractLiquid chromatography–mass spectrometry was applied to determine the action pattern of different chondroitin lyases. Two commercial enzymes, chondroitinase ABC (Proteus vulgaris) and chondroitinase ACII (Arthrobacter aurescens), having action patterns previously determined by viscosimetry and gel electrophoresis were first examined. Next, the action patterns of recombinant lyases, chondroitinase ABC from Bacteroides thetaiotaomicron (expressed in Escherichia coli) and chondroitinase AC from Flavobacterium heparinum (expressed in its original host), were examined. Chondroitin sulfate A (CS-A, also known as chondroitin-4-sulfate) was used as the substrate for these four lyases. Aliquots taken at various time points were analyzed. The products of chondroitinase ABC (P. vulgaris) and chondroitinase AC (F. heparinum) contained unsaturated oligosaccharides of sizes ranging from disaccharide to decasaccharide, demonstrating that both are endolytic enzymes. The products afforded by chondroitinase ABC (B. thetaiotaomicron) and chondroitinase ACII (A. aurescens) contained primarily unsaturated disaccharide. These two exolytic enzymes showed different minor products, suggesting some subtle specificity differences between the actions of these two exolytic lyases on chondroitin sulfate A.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.ab.2008.10.014
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofAnalytical Biochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleLiquid Chromatography-Mass Spectrometry to Study Chondroitin Lyase Action Pattern
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.ab.2008.10.014
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dcterms.isVersionOfhttps://doi.org/10.1016/j.ab.2008.10.014
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.pages57-64
rpi.description.volume385


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