Ti(IV) Binds to Human Serum Transferrin More Tightly Than Does Fe(III).

This article presents information on human serum transferrin (Tf) that holds a central place in the metabolism of Fe(III). Tf also binds other metal ions. The binding strength correlates with the acidity of the metal. Of the few ions predicted to bind more tightly than Fe(III), only Bi(III) has been...

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Publicado en:Journal of the American Chemical Society Vol. 127; no. 32; pp. 11218 - 11220
Autores principales: Tinoco, Arthur D., Valentine, Ann M.
Formato: Artículo
Publicado: American Chemical Society 8/17/2005
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Acceso en línea:Ver este registro en EBSCOhost
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      dt: 8/17/2005
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        atl: Ti(IV) Binds to Human Serum Transferrin More Tightly Than Does Fe(III).
      aug:
        au:
          Tinoco, Arthur D.
          Valentine, Ann M.
        affil: Department of Chemistry, Yale University, P.O. Box 208107, New Haven, Connecticut 06520-8107.
      su:
        Transferrin
        Serum
        Iron metabolism
        Electrons
        Titanium
        Ions
        Carrier proteins
      sug:
        subj:
          Transferrin
          Serum
          Iron metabolism
          Electrons
          Titanium
          Ions
          Carrier proteins
      ab: This article presents information on human serum transferrin (Tf) that holds a central place in the metabolism of Fe(III). Tf also binds other metal ions. The binding strength correlates with the acidity of the metal. Of the few ions predicted to bind more tightly than Fe(III), only Bi(III) has been investigated, and its binding is weaker, probably because of its large size. Titanium(IV) is nearly the same size as Fe(III) and is a stronger hard Lewis acid. Titanium(IV) binding to transferrin is implicated in the bioactivity of Titanium-containing anticancer drugs and the plasma binding of Titanium from imaging reagents and implants.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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