Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity
Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity
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DOI：
10.1007/s00775-007-0244-8
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发表时间：
2007-08-01
影响因子：
3
通讯作者：
Bal, Wojciech
中科院分区：
文献类型：
--
作者：
Rozga, Malgorzata;Sokolowska, Magdalena;Bal, Wojciech
在100 mM NaCl和100 mM N-（2-羟乙基）哌嗪-N '-乙磺酸（Hepes）中，使用次氮基三乙酸（NTA）作为竞争剂，通过竞争性紫外-可见光谱滴定法直接测定了pH 7.4时Cu（II）在人血清白蛋白（HSA）N-末端位点（NTS）结合的条件稳定常数。测定溶于100 mM NaCl的HSA的log K（c）（NTS）值为12.0 +/- 0.1。由于三元Cu（NTA）（Hepes）络合物的形成，在100 mM Hepes缓冲液中获得11.4 +/-0.1的假log log K-NTS（c）值。HSA的皮摩尔亲和力Cu（II）对这些离子在神经退行性疾病的可用性的影响进行了简要讨论。
The conditional stability constant at pH 7.4 for Cu(II) binding at the N-terminal site (NTS) of human serum albumin (HSA) was determined directly by competitive UV-vis spectroscopy titrations using nitrilotriacetic acid (NTA) as the competitor in 100 mM NaCl and 100 mM N-( 2- hydroxyethyl) piperazine-N'-ethanesulfonic acid (Hepes). The log K (c)(NTS) value of 12.0 +/- 0.1 was determined for HSA dissolved in 100 mM NaCl. A false log log K-NTS(c) value of 11.4 +/- 0.1 was obtained in the 100 mM Hepes buffer, owing to the formation of a ternary Cu(NTA)( Hepes) complex. The impact of the picomolar affinity of HSA for Cu(II) on the availability of these ions in neurodegenerative disorders is briefly discussed.