首页> 外文期刊>Biological Trace Element Research >Biological Activation of Heteropoly Complex of Molybdotungstosilicate Containing Lanthanum K10H3La(SiMo6W5O39)2⋅26H2O: Spectroscopic Approach and Microcalorimetry
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Biological Activation of Heteropoly Complex of Molybdotungstosilicate Containing Lanthanum K10H3La(SiMo6W5O39)2⋅26H2O: Spectroscopic Approach and Microcalorimetry

机译:含镧K 10 H 3 La(SiMo 6 W 5 O 的钼酸钨硅酸盐杂多配合物的生物活化> 39 2 ⋅26H 2 O:光谱法和微量热法

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In this paper, the biological activation of heteropoly complex of molybdotungstosilicate containing lanthanum K10H3La(SiMo6W5O39)2⋅26H2O (LaW5) was investigated by spectroscopic approach and microcalorimetry under the human physiological conditions. Fluorescence spectroscopy in combination with UV–Vis absorption spectroscopy was employed to investigate the binding of LaW5 to bovine serum albumin (BSA). In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LaW5 is a result of the formation of LaW5–BSA complex. Binding parameters were determined using the Stern–Volmer equation. The results of thermodynamic parameters ∆G, ∆H, ∆S at different temperatures indicate that van der Waals interactions and hydrogen bonds play a major role for LaW5–BSA association. The distance r between donor (BSA) and acceptor (LaW5) was obtained according to fluorescence resonance energy transfer. Furthermore, the calorimetric method was used to monitor the biological activity of LaW5 in Escherichia coli.
机译:本文研究了含镧K 10 H 3 La(SiMo 6 W 5 用分光光度法和微量热法研究了sub> O 39 2 ⋅26H 2 O(LaW 5 )人类的生理状况。荧光光谱结合紫外可见吸收光谱研究了LaW 5 与牛血清白蛋白(BSA)的结合。在机理讨论中,证明了LaW 5 对BSA的荧光猝灭是LaW 5 -BSA配合物形成的结果。使用Stern-Volmer方程确定结合参数。不同温度下的热力学参数∆G,∆H,∆S的结果表明,范德华相互作用和氢键在LaW 5 -BSA缔合中起主要作用。根据荧光共振能量转移获得供体(BSA)与受体(LaW 5 )之间的距离r。此外,采用量热法监测LaW 5 在大肠杆菌中的生物学活性。

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