| 头孢噻肟-Cu(Ⅱ)-牛血清白蛋白相互作用的荧光光谱法研究 |
| |
| 引用本文： | 安娜,敖登高娃.头孢噻肟-Cu(Ⅱ)-牛血清白蛋白相互作用的荧光光谱法研究[J].分析试验室,2012,31(2):38-40. |
| |
| 作者姓名： | 安娜 敖登高娃 |
| |
| 作者单位： | 内蒙古大学化学化工学院,010021 |
| |
| 基金项目： | 内蒙古自然科学基金，内蒙古大学"211"创新人才培养项目 |
| |
| 摘 要： | 用荧光光谱法研究了生理酸度条件下,头孢噻肟对牛血清白蛋白,Cu(Ⅱ)对牛血清白蛋白以及Cu(Ⅱ)对头孢噻肟和牛血清白蛋白荧光光谱特性的影响。结果表明:Cu(Ⅱ)和头孢噻肟均可使牛血清白蛋白的荧光强度发生静态猝灭,并且在Cu(Ⅱ)存在下,头孢噻肟对牛血清白蛋白的荧光猝灭作用显著增强。根据荧光猝灭双倒数图计算头孢噻肟和牛血清白蛋白的结合常数为3.11×104L/mol,结合位点数为1.03;二元配合物Cu(Ⅱ)与牛血清白蛋白之间的结合常数为1.13×103L/mol,结合位点数为0.74。
|
| 关 键 词： | 荧光光谱法 头孢噻肟 牛血清白蛋白 Cu(Ⅱ) 相互作用. |
Interaction of cefotaxime with human serum albumin: Investigation by fluorescence spectroscopy |
| |
| AN Na
,
Aodegaowo.Interaction of cefotaxime with human serum albumin: Investigation by fluorescence spectroscopy[J].Chinese Journal of Analysis Laboratory,2012,31(2):38-40. |
| |
| Authors: | AN Na Aodegaowo |
| |
| Institution: | AN Na and Aodegaowo(college of chemistry and chemical Engineering,Inner Mongolia University,Hohht 010021) |
| |
| Abstract: | The binding characteristics of cefotaxime(CTX),Cu(Ⅱ)and BSA have been studied by fluorescence spectroscopy in physiological pH conditions.The results showed that both Cu(Ⅱ) and CTX could quench the fluorescence intensity of BSA via a nonradiative energy transfer mechanism.Moreover,CTX could quench the fluorescence of BSA significantly in the presence of Cu(Ⅱ).The binding constants(K) and the binding sites(n) were calculated after analyzing fluorescence quenching data with double-reciprocal equation.The K and n between CTX and BSA were 3.11×104L/mol and 1.03,respectively in the CTX-BSA complex,while the K and n between Cu(Ⅱ) and BSA were 1.13×103 L/mol and 0.74 respectively in the binary complex of Cu(Ⅱ) and BSA. |
| |
| Keywords: | Fluorescence spectroscopy Cefotaxime(CTX) Copper(Ⅱ) Bovine serum albumin Interaction |
| 本文献已被 CNKI 万方数据 等数据库收录！ |
