Binding patterns of vanadium ions with different valence states to human serum transferrin studied by HPLC/high-resolution ICP-MS
DOI: 10.1016/S0006-291X(02)02067-3
Title: Binding patterns of vanadium ions with different valence states to human serum transferrin studied by HPLC/high-resolution ICP-MS
Journal Title: Biochemical and Biophysical Research Communications
Volume: 296
Issue: 5
Publication Date: 6 September 2002
Start Page: 1207
End Page: 1214
Published online: online 28 August 2002
ISSN: 0006-291X
Affiliations:
  • National Institute of Health Sciences, Kamiyoga 1-18-1, Setagaya, Tokyo 158-8501, Japan
  • Abstract: (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) ≌ 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.
    Received: 23 June 2002
    Keywords: Transferrin; Vanadium; Valence state; High-resolution inductively coupled plasma-mass spectrometry; ICP-MS; HR-ICP-MS; Binding affinity; Open form
    Email: maitani@nihs.go.jp

    Please Share this Paper with friends:
    Comment
    No.
    Comment Content
    User Name
    Date
    Post new Comment
    UserName