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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
纸质出版日期:2016-11-5,
收稿日期:2016-5-10,
修回日期:2016-6-17,
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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.
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。
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.
作用机制转铁蛋白光谱法头孢噻肟钠
interaction mechanismtransferrinspectroscopycefotaxime sodium
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