An in vitro study on the binding of Al(III) to human serum transferrin with the isoelectric focusing technique |
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Authors: | G. de Jong C. C. A. Ammerlaan W. L. van Noort H. G. van Eijk G. L. van Landeghem P. C. D'Haese M. E. de Broe |
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Affiliation: | (1) Department of Chemical Pathology, Faculty of Medicine, Erasmus University Rotterdam, The Netherlands;(2) Department of Internal Medicine II, Academic Hospital Rotterdam, Erasmus University Rotterdam, The Netherlands;(3) Department of Chemical Pathology, Faculty of Medicine, Erasmus University Rotterdam, Dr Molewaterplein 50, 3015 GE Rotterdam, The Netherlands;(4) Department of Nephrology-Hypertension, University of Antwerpen, Belgium |
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Abstract: | Transferrin saturated with Al3+ subjected to isoelectric focusing (IEF) in a pH gradient can be separated into four fractions, representing the apotransferrin, transferrin with aluminum at the metal binding site in the C- or N-terminal lobe, or both. The electrophoretic mobilities of these four fractions are identical to those of the iron-transferrin counterparts. Simultaneous binding of aluminum and iron to transferrin can also be demonstrated. The decreased saturation after IEF indicates that the affinity of transferrin for aluminum is low compared with its affinity for iron. This effect is particularly evident when bicarbonate is used as the synergistic anion in the loading procedure. In contrast, loading of transferrin with aluminum in the presence of oxalate produces a di-aluminum-transferrin complex that is stable during IEF. |
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Keywords: | aluminum isoelectric focusing PhastSystem transferrin |
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