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• W1983311888 abstract "Vanadium (V) is an essential metal for mammals and has different valence states. In blood, V is bound to serum transferrin (Tf), a glycoprotein which has two metal-binding sites, and carbonate is generally required for the binding. In this study, the binding patterns of V(III), V(IV), and V(V) to human serum Tf (hTf) were analyzed using an HPLC system equipped with an anion-exchange column and directly connected to a high-resolution inductively coupled plasma-mass spectrometer for metal detection (51V). In affinity to hTf, the three ions were ranked V(III)>V(IV)>V(V) in the presence of bicarbonate and V(III) reverse congruent V(IV)>V(V) in the absence. Intermediates in the open forms binding to the respective sites were detected at the initial stage. V(IV) and V(V) were bound to the N-lobe site in the closed form and open form, respectively. In the absence of bicarbonate, V ions with respective valence states were bound to hTf in the open form. In terms of binding to hTf, tri-valent V was most favorable in the presence of bicarbonate." @default.
• W1983311888 created "2016-06-24" @default.
• W1983311888 creator A5034836717 @default.
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• W1983311888 date "2002-09-01" @default.
• W1983311888 modified "2023-10-02" @default.
• W1983311888 title "Binding patterns of vanadium ions with different valence states to human serum transferrin studied by HPLC/high-resolution ICP-MS" @default.
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• W1983311888 doi "https://doi.org/10.1016/s0006-291x(02)02067-3" @default.
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