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dc.contributor.authorMach, Henryk
dc.contributor.authorVolkin, David B.
dc.contributor.authorBurke, Carl J.
dc.contributor.authorMiddaugh, C. Russell
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorFromm, Jonathan R.
dc.contributor.authorLoganathan, Duraikkannu
dc.contributor.authorMattsson, Lars
dc.date1993
dc.date.accessioned2022-06-27T17:14:57Z
dc.date.available2022-06-27T17:14:57Z
dc.date.issued1993-01-01
dc.identifier.citationMach H, Volkin DB, Burke CJ, Middaugh CR, Linhardt RJ, Fromm JR, Loganathan D, Mattsson L. Nature of the interaction of heparin with acidic fibroblast growth factor. Biochemistry. 1993 May 25;32(20):5480-9. doi: 10.1021/bi00071a026. PMID: 7684608.
dc.identifier.issn15204995
dc.identifier.issn62960
dc.identifier.urihttps://doi.org/10.1021/bi00071a026
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5982
dc.descriptionBiochemistry, 32, 5480-5489
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.abstractThe binding of human acidic fibroblast growth factor (aFGF) to heparin has been analyzed by a variety of different approaches to better elucidate the nature of this protein/sulfated polysaccharide interaction. Static and dynamic light scattering as well as analytical ultracentrifugation analyses indicates that 14-15 molecules of a FGF can bind to a 16-kDa heparin chain, with approximately 10 of these bound relatively uniformly to high-affinity sites. The dissociation constants of these latter sites are estimated to be approximately 50-140 nM on the basis of surface plasmon resonance experiments in which the association and dissociation rates of aFGF interaction with immobilized heparin were measured. The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides. The smallest aFGF-protected oligosaccharide comigrated with delta UA2S(1-->4)-alpha-D-GlcNp2S6S(1-->4)-alpha-L-IdoAp-2S( 1-->4)-alpha-D-GlcNp2S6S (where delta UA represents 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid and S is sulfate). Thus, aFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin. This potentially provides a concentrated, stabilized storage form of the growth factor that can be released for receptor-mediated cellular activation in response to the proper stimuli. It is also possible that close proximity of aFGF molecules on the highly sulfated regions of heparan chains may be involved in the induction of receptor aggregation as suggested by Ornitz et al. [Ornitz, D. M., Yayon, A., Flanagan, J. G., Svahn, C. M., Levi, E., & Leder, P. (1992) Mol. Cell. Biol. 12, 240-247].
dc.description.sponsorshipNational Institute of General Medical Sciences
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi00071a026
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleNature of the Interaction of Heparin with Acidic Fibroblast Growth Factor
dc.typeArticle
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dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/bi00071a026
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.pages5480-5489
rpi.description.volume32


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