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ADSORPTION OF HUMAN RECOMBINANT FIBRONECTIN TO TITANIUM IN VITRO

DC Field Value Language
dc.contributor.authorKim, H.J.-
dc.contributor.authorChang, I.T-
dc.contributor.authorKoak, J.Y.-
dc.contributor.authorHeo, S.J.-
dc.contributor.authorYim, S.A.-
dc.contributor.authorJang, J.H-
dc.date.accessioned2010-02-01T09:47:06Z-
dc.date.available2010-02-01T09:47:06Z-
dc.date.issued2004-
dc.identifier.citation2004;42;3en
dc.identifier.issn0301-2875-
dc.identifier.urihttps://hdl.handle.net/10371/47712-
dc.description.abstractStatement of problem. Fibronectin mediates its biological effects by binding to integrins on cell membranes through a consensus site including the Arg-Gly-Asp (RGD) sequence within tenth type III module. Purpose. The purpose of our study was to investigate the adsorption affinity of human recombinant fibronectin peptide (hFNIII 9-10) to titanium and to investigate the effect of the surrounding ionic composition on the adsorption process. Material and methods. As for evaluating the affinity of hFNIII 9-10 to Ti, titanium disks were incubated in 40, 80 and hFNIII 9-10 solution at overnight, repectively. As for evaluating the effect of surrounding ionic concentration, hFNIII 9-10 was dissolved in distilled water, phosphate buffered saline and RPMI 1640. Optical density (O.D.) was measured in ELISA reader. Results. The results were as follows; 1. The adsorption of hFNIII 9-10 showed significantly highest mean optical density (O.D.) value in . 2. The difference of ionic composition in DW, PBS and RPMI did not influence the adsorption amount of hFNIII 9-10.en
dc.description.sponsorshipThis work was supported by the korea Science and Engineering Foundation through the intellectual Biointerface Engineering Center at Seoul National University.en
dc.language.isoenen
dc.publisher대한치과보철학회en
dc.subjectFibronectinen
dc.subjectTitaniumen
dc.titleADSORPTION OF HUMAN RECOMBINANT FIBRONECTIN TO TITANIUM IN VITROen
dc.typeArticleen
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