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    The proteoglycan bikunin has a defined sequence

    Author
    Ly, Mellisa; Leach, Franklin E.; Laremore, Tatiana N.; Toida, Toshihiko; Amster, I. Jonathan; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    THE PROTEOGLYCAN BIKUNIN HAS A DEFINED SEQUENCE.pdf (971.7Kb)
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    Date Issued
    2011-01-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In 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/;
    Full Citation
    The 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.
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    URI
    https://hdl.handle.net/20.500.13015/5279; https://doi.org/10.1038/nchembio.673
    Abstract
    Proteoglycans 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.;
    Description
    Nature Chemical Biology, 7, 827-833; Note : 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.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    Nature
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Nature Chemical Biology; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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