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Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS by Megumi Hamano Nagaoka; Tamio Maitani is a Chemistry article available to read on EtoBox.
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Aluminium (Al) in the blood is bound to transferrin (Tf), a glycoprotein of about 80 kDa that is characterized by its need for a synergistic anion. In this focused review, the binding affinity of Al to Tf is surveyed in the context of our recent studies using on-line high-performance liquid chromatography/high-resolution inductively coupled plasma mass spectrometry (HPLC/HR-ICP-MS). Al in human serum without any in vitro Al-spikes was present in a form bound to the N-lobe site of Tf. The influences of sialic acid in the carbohydrate chain of human serum Tf (hTf) were studied using asialo-hTf, obtained by treatment with sialidase. The binding affinity of Fe was similar between asialo-hTf and native-hTf, while that of Al for asialo-hTf was larger than that for native-hTf, especially in the presence of oxalate, a synergistic anion. The above findings are discussed in relation to diseases in which the serum concentrations of carbohydrate-deficient Tf and oxalate are augmented.
Who reads Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS?
It is typically read by researchers, students, and practitioners in Chemistry.
- Author
- Megumi Hamano Nagaoka; Tamio Maitani
- Publisher
- Elsevier Science; Elsevier ; Elsevier BV (ISSN 0162-0134)
- Published
- 2005
- Language
- EN
- Field
- Chemistry (Physical Sciences)