首页> 外文期刊>Journal of the Chinese Chemical Society >Investigation of the Interaction between N,N'-di(4-chlorophenyl)thiourea and Human Serum Albumin by Fluorescence Spectroscopy: Synchronous Fluorescence Determination of Human Serum Albumin
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Investigation of the Interaction between N,N'-di(4-chlorophenyl)thiourea and Human Serum Albumin by Fluorescence Spectroscopy: Synchronous Fluorescence Determination of Human Serum Albumin

机译:N,N'-二(4-氯苯基)硫脲与人血清白蛋白相互作用的荧光光谱研究:同步荧光法测定人血清白蛋白

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摘要

Under physiological conditions, interaction between N,N'-di(4-chlorophenyl)thiourea synthesized and human serum albumin was investigated by using fluorescence spectroscopy and UV absorption spectrum. The intrinsic fluorescence of human serum albumin was quenched by N,N'-di(4-chlorophenyl)-thiourea through a static quenching procedure. The binding constants (K) at 14℃ and 24℃ were obtained, and the values were 2.541 x 10~5 M~(-1) and 2.021 x 10~5 M~(-1), respectively. Thermodynamic parameter enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -16.19 KJ/mol and 47.05 J·mol~(-1)·K~(-1), respectively, which indicated that hydrophobic force played a major role in interaction. The binding distance was evaluated on the basis of the theory of Foster energy transfer. The effects of various metal ions on the binding constants of N,N'-di(4-chlorophenyl)thiourea with human serum albumin were studied. A synchronous fluorescence technique for determination of human serum albumin was developed, and the method was successfully applied to the detection of HSA in human serum samples.
机译:在生理条件下,利用荧光光谱和紫外吸收光谱研究了合成的N,N'-二(4-氯苯基)硫脲与人血清白蛋白之间的相互作用。 N,N'-二(4-氯苯基)-硫脲通过静态淬灭程序淬灭人血清白蛋白的固有荧光。得到了14℃和24℃的结合常数(K),分别为2.541×10〜5M〜(-1)和2.021×10〜5M〜(-1)。热力学参数焓变(ΔH)和熵变(ΔS)经计算分别为-16.19 KJ / mol和47.05 J·mol〜(-1)·K〜(-1),表明疏水力起了主要作用。在互动中的作用。结合距离基于Foster能量转移理论进行评估。研究了各种金属离子对N,N'-二(4-氯苯基)硫脲与人血清白蛋白结合常数的影响。开发了一种同步荧光测定人血清白蛋白的方法,并将该方法成功地用于人血清中HSA的检测。

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