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dc.contributor.authorZhao, J.
dc.contributor.authorKong, Y.
dc.contributor.authorZhang, F.
dc.contributor.authorLinhardt, Robert J.
dc.date2018
dc.date.accessioned2022-06-23T04:28:42Z
dc.date.available2022-06-23T04:28:42Z
dc.date.issued2018
dc.identifier.citationImpact of temperature on heparin and protein interactions, J. Zhao, Y. Kong, F. Zhang, R. J. Linhardt, Biochemistry and Physiology, 7, 2, 2018.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5374
dc.identifier.urihttps://doi.org/10.4172/2168-9652.1000241
dc.descriptionBiochemistry and Physiology, 7, 2
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.abstractHeparin has many important biological activities, associated with a diverse set of interactions with biologically functional proteins. The binding mechanisms and biological significance of heparin-protein interactions have attracted wide attention. However, the temperature sensitivity of heparin-protein interaction is relatively unstudied. The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. The affinity and kinetics of these interactions were measured at 10°C, 25°C and 30°C. The association rate, dissociation rate, binding affinity and binding mass were compared at different temperatures. In the two state binding process between AT III and heparin, temperature played a negligible role on ATIII binding to heparin (1st state reaction), but demonstrated a role in the conformational change process (2nd state reaction). In the case of FGF1 and FGF2, the kinetics and affinity, while distinctly different at the temperatures studies, were still within the same order of magnitude. Based these results, we conclude that it many cases it is possible to perform surface plasmon resonance measurements of heparin-protein interaction at different temperatures, especially at reduced (ambient or lower) temperatures, and obtain comparable binding data.
dc.languageen_US
dc.language.isoENG
dc.publisherOmics
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleImpact of temperature on heparin and protein interactions
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.4172/2168-9652.1000241
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)


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