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dc.contributor.authorWilliams, A.
dc.contributor.authorHe, W.
dc.contributor.authorCress, B.F.
dc.contributor.authorLiu, X.
dc.contributor.authorAlexandria, J.
dc.contributor.authorYoshizawa, H.
dc.contributor.authorNishimura, Kazuhiro
dc.contributor.authorToida, T.
dc.contributor.authorKoffas, M.
dc.contributor.authorLinhardt, Robert J.
dc.date2017
dc.date.accessioned2022-06-23T04:28:43Z
dc.date.available2022-06-23T04:28:43Z
dc.date.issued2017
dc.identifier.citationCloning and expression of recombinant chondroitinase AC II and its comparison to the Arthrobacter aurescens enzyme, A. Williams, W. He, B. F. Cress, X. Liu, J. Alexandria, H. Yoshizawa, K. Nishimura, T. Toida, M. Koffas, R. J. Linhardt, Biotechnology Journal, 12, 1700239, 2017.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5380
dc.identifier.urihttps://doi.org/10.1002/biot.201700239
dc.descriptionBiotechnology Journal, 12, 1700239
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.abstractChondroitin sulfates are the glycosaminoglycan chains of proteoglycans critical in the normal development and pathophysiology of all animals. Chondroitinase ACII, a polysaccharide lyase originally isolated from Arthrobacter aurescens IAM 110 65, which is widely used in the analysis and study of chondroitin structure, is no longer commercially available. The aim of the current study is to prepare recombinant versions of this critical enzyme for the glycobiology research community. Two versions of recombinant chondroitinase ACII are prepared in Escherichia coli, and their activity, stability, specificity, and action pattern are examined, along with a non-recombinant version secreted by an Arthrobacter strain. The recombinant enzymes are similar to the enzyme obtained from Arthrobacter for all examined properties, except for some subtle specificity differences toward uncommon chondroitin sulfate substrates. These differences are believed to be due to either post-translational modification of the Arthrobacter-secreted enzyme or other subtle structural differences between the recombinant and natural enzymes. The secreted chondroitinase can serve as a suitable replacement for the original enzyme that is currently unavailable, while the recombinant ones can be applied generally in the structural determination of most standard chondroitin sulfates.
dc.languageen_US
dc.language.isoENG
dc.publisherWiley
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleCloning and expression of recombinant chondroitinase AC II and its comparison to the Arthrobacter aurescens enzyme
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1002/biot.201700239
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)


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