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Cornplexation of Cm(III) with blood serum proteins: recombinant human serum albumin (rHSA)

The complexation of Cm(III) with the recombinant human serum albumin (rHSA) (characterized by single deletion of residue Asp-1), is studied in dependence of pH and rHSA concentration using time-resolved laser fluorescence spectroscopy (TRLFS). A Cm(III) rHSA species is formed between pH 6.4 and 10.0...

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Hauptverfasser: Adam, Nicole (VerfasserIn) , Reitz, Cedric Y. (VerfasserIn) , Ditter, Anna-Lena (VerfasserIn) , Panak, Petra (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: May 26, 2021
In: Radiochimica acta
Year: 2021, Jahrgang: 109, Heft: 7, Pages: 547-550
ISSN:2193-3405
DOI:10.1515/ract-2021-1029
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1515/ract-2021-1029
Verlag, lizenzpflichtig, Volltext: https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=DOISource&SrcApp=WOS&KeyAID=10.1515%2Fract-2021-1029&DestApp=DOI&SrcAppSID=E1Ds9d5qwGMRH1DGxTT&SrcJTitle=RADIOCHIMICA+ACTA&DestDOIRegistrantName=Walter+de+Gruyter+GmbH
Volltext
Verfasserangaben:Nicole Adam, Cedric Y. Reitz, Anna-Lena Ditter and Petra J. Panak
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Zusammenfassung:The complexation of Cm(III) with the recombinant human serum albumin (rHSA) (characterized by single deletion of residue Asp-1), is studied in dependence of pH and rHSA concentration using time-resolved laser fluorescence spectroscopy (TRLFS). A Cm(III) rHSA species is formed between pH 6.4 and 10.0 with the conditional stability constant being logK = 6.47 at pH = 7.4. Competition titration experiments with Cu(II) and Zn(II) confirm complexation at the N-terminal binding site (NTS) of rHSA and exclude the involvement of the Multi-Metal Binding Site (MBS). Comparison with a previous study on Cm(III) interaction with native albumin, HSA, points out, that residue Asp-1 is involved in Cm(III) binding to HSA but is not crucial for Cm(III) complexation at the NTS. The results are of major importance for a better understanding of fundamental actinide-protein interaction mechanisms which are highly required for the identification and characterization of relevant distribution pathways of incorporated radionuclides.
Beschreibung:Gesehen am 10.08.2021
Beschreibung:Online Resource
ISSN:2193-3405
DOI:10.1515/ract-2021-1029

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