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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Spectroscopic studies on the interaction between riboflavin and albumins
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Spectroscopic studies on the interaction between riboflavin and albumins

机译：核黄素与白蛋白相互作用的光谱研究

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摘要

The interactions between riboflavin (RF)and human and bovine serum albumin (HSA and BSA) were studied by using absorption and fluorescence spectroscopic methods. Intrinsic fluorescence emission spectra of serum albumin in the presence of RF show that the endogenous photosensitizer acts as a quencher. The decrease of fluorescence intensity at about 350 urn is attributed to changes in the environment of the protein fluorophores caused by the ligand. The quenching mechanisms of albumins by RF were discussed. The binding constants and binding site number were obtained at various temperatures. The distance between albumins and RF in the complexes suggests that the primary binding site for RF is close to tryptophan residue (Trp214) of HSA and Trp212 of BSA. The hydration process of albumins has also been discussed. (c) 2006 Elsevier B.V. All rights reserved.
机译：通过吸收和荧光光谱法研究了核黄素（RF）与人和牛血清白蛋白（HSA和BSA）之间的相互作用。射频存在下血清白蛋白的内在荧光发射光谱表明，内源性光敏剂可作为淬灭剂。大约350微米时荧光强度的降低归因于配体引起的蛋白质荧光团环境的变化。讨论了RF对白蛋白的猝灭机理。在不同温度下获得结合常数和结合位点数。复合物中白蛋白和RF之间的距离表明，RF的主要结合位点靠近HSA的色氨酸残基（Trp214）和BSA的Trp212。还讨论了白蛋白的水合过程。 （c）2006 Elsevier B.V.保留所有权利。

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