Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS--speciation of aluminium in human serum.
Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS--speciation of aluminium in human serum.
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DOI：
10.1016/j.jinorgbio.2005.06.034
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发表时间：
2005-09
影响因子：
3.9
通讯作者：
M. Nagaoka;T. Maitani
中科院分区：
文献类型：
--
作者：
M. Nagaoka;T. Maitani
血液中的铝（Al）与转铁蛋白（Tf）结合，转铁蛋白是一种约80 kDa的糖蛋白，其特征在于需要协同阴离子。在这个集中的审查，铝Tf的结合亲和力调查的背景下，我们最近的研究，使用在线高效液相色谱/高分辨率电感耦合等离子体质谱（HPLC/HR-ICP-MS）。在人血清中没有任何在体外铝尖峰铝是以结合到Tf的N-叶位点的形式存在。使用唾液酸酶处理获得的唾液酸-hTf研究了唾液酸对人血清转铁蛋白（hTf）糖链的影响。Fe的结合亲和力在去唾液酸-hTf和天然-hTf之间相似，而Al对去唾液酸-hTf的结合亲和力大于天然-hTf，特别是在存在草酸根的情况下，草酸根是一种协同阴离子。上述研究结果进行了讨论有关的疾病，其中血清中的碳水化合物缺乏转铁蛋白和草酸的浓度增加。
Aluminium (Al) in the blood is bound to transferrin (Tf), a glycoprotein of about 80kDa 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.