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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bauer, Nicole Fröhlich, Daniel R. Panak, Petra J. |
| Description | Author Affiliation: Bauer N ( Karlsruhe Institute of Technology (KIT), Campus North, Institute for Nuclear Waste Disposal (INE), P.O. Box 3640, 76021 Karlsruhe, Germany. Nicole.bauer@kit.edu.) |
| Abstract | The complexation of Cm(III) with human serum transferrin was investigated in a pH range from 3.5 to 11.0 using time-resolved laser fluorescence spectroscopy (TRLFS). At pH ≥ 7.4 Cm(III) is incorporated at the Fe(III) binding site of transferrin whereas at lower pH a partially bound Cm(III) transferrin species is formed. At physiological temperature (310 K) at pH 7.4, about 70% of the partially bound and 30% of the incorporated Cm(III) transferrin species are present in solution. The Cm(III) results obtained by TRLFS are in very good agreement with Am(III) EXAFS results, confirming the incorporation of Am(III) at the Fe(III) binding site at pH 8.5. |
| ISSN | 14779226 |
| Issue Number | 18 |
| Volume Number | 43 |
| e-ISSN | 13645447 |
| Journal | Dalton Trans. |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Publisher Date | 2014-05-14 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Subscribed |
| Subject Keyword | Fluoroimmunoassay Transferrin Analysis Metabolism X-Ray Absorption Spectroscopy Curium Methods Humans Protein Binding Physiology Journal Article Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Inorganic Chemistry |
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