Spectral Properties of The Interaction Between Transferrin and Cefotaxime Sodium

CUI Meng-meng; LIU Bao-sheng; LI Tong-tong; DUAN Shao-tong

doi:10.3788/fgxb20163711.1415

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Spectral Properties of The Interaction Between Transferrin and Cefotaxime Sodium

更新时间：2020-08-12

- Spectral Properties of The Interaction Between Transferrin and Cefotaxime Sodium
- Chinese Journal of Luminescence Vol. 37, Issue 11, Pages: 1415-1421(2016)
- 作者机构：
  
  河北大学化学与环境科学学院河北省分析科学技术重点实验室, 河北保定 071002
- 作者简介：
- 基金信息：
- DOI：10.3788/fgxb20163711.1415
  CLC： O657.3
- Received：10 May 2016，
  
  Revised：17 June 2016，
  
  Published：05 November 2016
- 稿件说明：
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崔萌萌, 刘保生, 李彤彤等. 头孢噻肟钠、转铁蛋白相互作用的光谱特征[J]. 发光学报, 2016,37(11): 1415-1421

CUI Meng-meng, LIU Bao-sheng, LI Tong-tong etc. Spectral Properties of The Interaction Between Transferrin and Cefotaxime Sodium[J]. Chinese Journal of Luminescence, 2016,37(11): 1415-1421
崔萌萌, 刘保生, 李彤彤等. 头孢噻肟钠、转铁蛋白相互作用的光谱特征[J]. 发光学报, 2016,37(11): 1415-1421 DOI： 10.3788/fgxb20163711.1415.

CUI Meng-meng, LIU Bao-sheng, LI Tong-tong etc. Spectral Properties of The Interaction Between Transferrin and Cefotaxime Sodium[J]. Chinese Journal of Luminescence, 2016,37(11): 1415-1421 DOI： 10.3788/fgxb20163711.1415.

摘要

将转铁蛋白（TRF）的荧光变化作为研究对象，在298，310，318 K下采用紫外吸收、传统荧光、同步荧光、圆二色谱法，对TRF与头孢噻肟钠（CEM）的结合进行综合分析。数据处理和分析结果显示：TRF的荧光伴随CEM浓度的提高而呈现规律性猝灭，猝灭方式是静态的。两者借助静电作用结合，反应生成新物质。结果的准确性通过上述方法进行了验证。此外，同步荧光和圆二色谱也表明CEM影响了TRF的构象。

Abstract

The interaction between transferrin (TRF) and cefotaxime sodium (CEM) at different temperatures (298

310 and 318 K) was studied by using UV absorption spectroscopy

traditional fluorescence spectroscopy

synchronous fluorescence spectroscopy and circular dichroism spectroscopy. The experiment results indicate that the fluorescence of TRF is regularly quenched with the addition of CEM. The quenching pattern is static. TRF and CEM are combined by electrostatic interaction

and new compound forms during the process. These different methods verify the accuracy and rationality of the results. In addition

synchronous fluorescence spectroscopy and circular dichroism spectroscopy both show the conformation of TRF is influenced by CEM.

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references

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