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    Isolation of bovine corneal keratan sulfate and its growth factor and morphogen binding

    Author
    Weyers, Amanda; Yang, Bo; Solakyildirim, Kemal; Yee, Vienna; Li, Lingyun; Zhang, Fuming; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    ISOLATION OF BOVINE CORNEAL KERATAN SULFATE AND ITS GROWTH FACTOR.pdf (3.027Mb)
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    Date Issued
    2013-05-01
    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
    Isolation of bovine corneal keratan sulfate and its growth factor and morphogen binding,A. Weyers, B. Yang, K. Solakyildirim, V. Yee, L. Li, F. Zhang, R. J. Linhardt, FEBS Journal, 280, 2285–2293, 2013.
    Metadata
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    URI
    https://hdl.handle.net/20.500.13015/5299; https://doi.org/10.1111/febs.12165
    Abstract
    Keratan sulfate (KS) is an important glycosaminoglycan that is found in cartilage, reproductive, and neural tissues. Corneal KS glycosaminoglycan is found N-linked to lumican, keratocan, and mimecan proteoglycans and has been widely studied by investigators interested in corneal development and diseases. Recently, the availability of corneal KS has become severely limited due to restricted the shipment of bovine central nervous system by-products across international borders in efforts to prevent additional cases of mad cow disease. We report a simple method for the purification of multi-milligram quantities of bovine corneal KS and characterize its structural properties. We also examined its protein-binding properties and discovered that corneal KS bound with high affinity to fibroblast growth factor-2 and sonic hedgehog, a growth factor and a morphogen involved in corneal development and healing.;
    Description
    FEBS Journal, 280, 2285–2293; 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
    FEBS Press
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; FEBS Journal; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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