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dc.contributor.authorHe, Wenqin
dc.contributor.authorZhu, Yuanyuan
dc.contributor.authorShirke, Abhijeet
dc.contributor.authorSun, Xiaojun
dc.contributor.authorLiu, Jian
dc.contributor.authorGross, Richard A.
dc.contributor.authorKoffas, Mattheos A.G.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorLi, Ming
dc.date2017
dc.date.accessioned2022-06-27T15:52:27Z
dc.date.available2022-06-27T15:52:27Z
dc.date.issued2017-09-01
dc.identifier.citationExpression of chondroitin-4-O-sulfotransferase in Escherichia coli and Pichia pastoris, W. He, Y. Zhu, A. Shirke, X. Sun, J. Liu, R. A. Gross, M. A. G. Koffas, R. J. Linhardt, M. Li, Applied Microbiology and Biotechnology, 101, 6919–6928, 2017.
dc.identifier.issn14320614
dc.identifier.issn1757598
dc.identifier.urihttps://doi.org/10.1007/s00253-017-8411-5
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5613
dc.descriptionApplied Microbiology and Biotechnology, 101, 6919–6928
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 linear sulfated polysaccharides called glycosaminoglycans. They are important nutraceutical and pharmaceutical products that are biosynthesized through the action of chondroitin sulfotransferases on either an unsulfated chondroitin or a dermatan polysaccharide precursor. While the enzymes involved in the biosynthesis of chondroitin sulfates are well known, the cloning end expression of these membrane-bound Golgi enzymes continue to pose challenges. The major chondroitin-4-sulfotransferase, Homo sapiens C4ST-1, had been previously cloned and expressed from mammalian CHO, COS-7, and HEK 293 cells, and its activity was shown to require glycosylation. In the current study, a C4ST-1 construct was designed and expressed in both Escherichia coli and Pichia pastoris in its non-glycosylated and glycosylated forms. Both constructs showed similar activity albeit different kinetic parameters when acting on a microbially prepared unsulfated chondroitin substrate. Moreover, the glycosylated form of C4ST-1 showed lower stability than the non-glycosylated form.
dc.description.sponsorshipNational Science Foundation
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s00253-017-8411-5
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofApplied Microbiology and Biotechnology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleExpression of chondroitin-4-O-sulfotransferase in Escherichia coli and Pichia pastoris
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s00253-017-8411-5
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dcterms.isVersionOfhttps://doi.org/10.1007/s00253-017-8411-5
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.pages6919-6928
rpi.description.volume101


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