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dc.contributor.authorYu, Haining
dc.contributor.authorMuñoz, Eva M.
dc.contributor.authorEdens, R. Erik
dc.contributor.authorLinhardt, Robert J.
dc.date2005
dc.date.accessioned2022-06-23T03:56:11Z
dc.date.available2022-06-23T03:56:11Z
dc.date.issued2005-11-15
dc.identifier.citationKinetic Studies on the Interaction of Heparin and Complement Proteins using Surface Plasmon Resonance, H. Yu, E.M. Muñoz, F. Zhang, R.E. Edens, R.J. Linhardt, Biochemica Biophysica Acta, Biochemica Biophysica Acta, 1726, 168-176, 2005.
dc.identifier.issn3044165
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5188
dc.identifier.urihttps://doi.org/10.1016/j.bbagen.2005.08.003
dc.descriptionBiochemica Biophysica Acta, Biochemica Biophysica Acta, 1726, 168-176
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 is a naturally occurring polysaccharide known to interact with complement proteins and regulate multiple steps in the complement cascade. Quantitative information, in the form of affinity constants for heparin-complement interactions, is not generally available and there are no reports of a comprehensive analysis using the same interaction method. Such information should improve our understanding of how exogenously administered pharmaceutical heparin and the related endogenous polysaccharide, heparan sulfate, regulate complement activation. The current study provides the first comprehensively analysis of the binding of various complement proteins to heparin using surface plasmon resonance (SPR). Complement proteins C1, C2, C3, C4, C5, C6, C7, C8, C9, C1INH, factor I, factor H, factor B and factor P all bind heparin but exhibit different binding kinetics and dissociation constants (Kd) ranging from 2 to 320 nM. By taking into account these Kd values and the serum concentrations of these complement proteins, the percentage of each binding to exogenously administered heparin was calculated and found to range from 2% to 41%. This study provides essential information required for the rational design of new therapeutic agents capable of regulating the complement activation.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochimica et Biophysica Acta - General Subjects
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleKinetic Studies on the Interaction of Heparin and Complement Proteins using Surface Plasmon Resonance
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.bbagen.2005.08.003
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.pages168-176
rpi.description.volume1726


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