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dc.contributor.authorLy, Mellisa
dc.contributor.authorLeach, Franklin E.
dc.contributor.authorLaremore, Tatiana N.
dc.contributor.authorToida, Toshihiko
dc.contributor.authorAmster, I. Jonathan
dc.contributor.authorLinhardt, Robert J.
dc.date2011
dc.date.accessioned2022-06-23T04:11:26Z
dc.date.available2022-06-23T04:11:26Z
dc.date.issued2011-01-01
dc.identifier.citationThe proteoglycan bikunin has a defined sequence, M. Ly, F. E. Leach III, T. N. Laremore, T. Toida, I. J. Amster, R.J. Linhardt, Nature Chemical Biology, 7, 827-833, 2011.
dc.identifier.issn15524469
dc.identifier.issn15524450
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5279
dc.identifier.urihttps://doi.org/10.1038/nchembio.673
dc.descriptionNature Chemical Biology, 7, 827-833
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.abstractProteoglycans are complex glycoconjugates that regulate critical biological pathways in all higher organisms. Bikunin, the simplest proteoglycan, with a single glycosaminoglycan chain, is a serine protease inhibitor used to treat acute pancreatitis. Unlike nucleic acids and proteins, whose synthesis is template driven, Golgi-synthesized glycosaminoglycans are not believed to have predictable or deterministic sequences. Bikunin peptidoglycosaminoglycans were prepared and fractionated to obtain a collection of size-similar and charge-similar chains. Fourier transform mass spectral analysis identified a small number of parent molecular ions corresponding to monocompositional peptidoglycosaminoglycans. Fragmentation using collision-induced dissociation unexpectedly afforded a single sequence for each monocompositional parent ion, unequivocally demonstrating the presence of a defined sequence. The biosynthetic pathway common to all proteoglycans suggests that even more structurally complex proteoglycans, such as heparan sulfate, may have defined sequences, requiring a readjustment in the understanding of information storage in complex glycans.
dc.description.sponsorshipFoundation for the National Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherNature
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofNature Chemical Biology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleThe proteoglycan bikunin has a defined sequence
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1038/nchembio.673
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.pages827-833
rpi.description.volume7


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