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Fluorometric probing on the binding of hematoxylin to serum albumin

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Abstract

The binding of a cell nucleus stain, hematoxylin (HTL), to bovine serum albumin (BSA) was studied by spectroscopy including fluorescence spectra, UV–Visible absorption, circular dichroism (CD) spectra, synchronous and three-dimensional fluorescence spectra. The results indicated that the binding had led to static fluorescence quenching, with non-radiation energy transfer happening within single molecule. The observed binding constant was calculated to be 105.588 l mol−1 at 311 K and one binding site had formed. The thermodynamic parameters of the interaction complied with ΔG θ < 0, ΔH θ < 0, ΔS θ < 0 and the results indicate that hydrogen bonds played major role in the reaction. The distance r between donor (BSA) and acceptor (HTL) was obtained according to the Förster theory of non-radiation energy transfer. The structural change of BSA molecules with addition of HTL was analyzed and the optimized geometry of HTL–BSA was investigated by fluorescence probe method.

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Authors and Affiliations

  1. College of Chemical and Pharmaceutical Engineering, Jingchu University of Technology, 448000, Jingmen, Hubei, People’s Republic of China

    Hua-xin Zhang, Song Gao, Ze-yun Xiong & Shan-pei Liu

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  1. Hua-xin Zhang
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  2. Song Gao
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Correspondence to Hua-xin Zhang.

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Zhang, Hx., Gao, S., Xiong, Zy. et al. Fluorometric probing on the binding of hematoxylin to serum albumin. Mol Biol Rep 36, 2299–2306 (2009). https://doi.org/10.1007/s11033-009-9448-z

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  • DOI: https://doi.org/10.1007/s11033-009-9448-z

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