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dc.contributor.authorVolkin, David B.
dc.contributor.authorTsai, P. K.
dc.contributor.authorDabora, Jonathan M.
dc.contributor.authorGress, Jacqueline O.
dc.contributor.authorBurke, Carl J.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorMiddaugh, C. Russell
dc.date1993
dc.date.accessioned2022-06-27T17:14:57Z
dc.date.available2022-06-27T17:14:57Z
dc.date.issued1993-01-01
dc.identifier.citationPhysical Stabilization of Acidic Fibroblast Growth Factor by Polyanions, D.B. Volkin, P.K. Tsai, J.M. Dabora, J.O. Gress, C.J. Burke, R.J. Linhardt, C.R. Middaugh, Archives in Biochemistry and Biophysics, 300, 30-41, (1993).
dc.identifier.issn39861
dc.identifier.urihttps://doi.org/10.1006/abbi.1993.1005
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5984
dc.descriptionArchives in Biochemistry and Biophysics, 300, 30-41,
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.abstractAcidic fibroblast growth factor (aFGF) is markedly stabilized by heparin. Partially due to the heterogeneity of heparin preparations, the nature of the aFGF polyanion binding site is still ill-defined. We have, therefore, investigated a wide variety of well-defined polyanions in terms of their ability to stabilize human recombinant aFGF (15-154) against thermal denaturation. The specificity of the interaction between aFGF and polyanions is shown to be remarkably weak with a surprising number of polyanions (including small phosphorylated and sulfated compounds as well as highly charged biopolymers) able to induce physical stability. Temperature-dependent fluorescence and circular dichroism measurements show that many of these polyanionic compounds stabilize aFGF to the same extent as heparin. The ability of these agents to protect the three free thiol groups of aFGF from copper-catalyzed oxidation was also explored and significant protection was observed. The extent and electrostatic requirements of the protein's polyanion binding site were probed by the use of a series of well-defined heparin fragments and differentially phosphorylated inositol compounds. A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation. Increasing phosphorylation of inositol compounds (up to six phosphate groups per molecule) enhances the thermal stability of aFGF. These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/abbi.1993.1005
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titlePhysical Stabilization of Acidic Fibroblast Growth Factor by Polyanions
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/abbi.1993.1005
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dcterms.isVersionOfhttps://doi.org/10.1006/abbi.1993.1005
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.pages30-41
rpi.description.volume300


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