节点文献

秋水仙碱与牛血清白蛋白相互作用的电化学研究

Study on the interaction between colchicine and bovine serum albumin using electrochemical method

  • 推荐 CAJ下载
  • PDF下载
  • 不支持迅雷等下载工具,请取消加速工具后下载。

【作者】 曹福悦; 任凤莲; 宋鸽; 蒲秋梅; 沈芳; 赵金尧;

【Author】 CAO Fu-yue,REN Feng-lian,SONG Ge,PU Qiu-mei,SHEN Fang and ZHAO Jin-yao(College of Chemistry and Chemical Engineering,Central South University,Changsha 410083)

【机构】 中南大学化学化工学院;

【摘要】 以电化学方法对秋水仙碱与牛血清白蛋白的相互作用进行了研究。在0.3 mol/L H2SO4底液中,秋水仙碱在玻碳电极上产生一不可逆的氧化峰,峰电位为1.18 V(vs.SCE),加入表面活性剂四丁基氯化铵后,秋水仙碱的峰信号得到明显提高。在上述条件下,加入BSA后秋水仙碱的氧化峰电位正移,峰电流下降,峰电流下降值与BSA加入的浓度在1.5×10-7~2×10-6mol/L(r=0.9978)范围内有良好的线性关系,检出限达4.0×10-8mol/L。进一步探讨了秋水仙碱与BSA的结合数和结合常数,得到结合数为1,结合常数为2.40×105L/mol。

【Abstract】 The electrochemical method has been used for study on the interaction between colchicine and bovine serum albumin in this paper.An irreversible oxidation peak of colchicine has been obtained in 0.3 mol/L H2SO4 solution.The peak potential is at 1.18 V(vs.SCE).The peak current significantly increased with the addition of the surfactant of tetrabutyl ammonium chloride.Under these conditions,the BSA,the oxidation peak potential shifted and the peak current decreased with the addition of BAS.The declining value of the peak current was directly proportional to the bovine serum albumin concentration in the range of 1.5×10-7~2×10-6 mol/L(r=0.9978).The detection limit was 4.0×10-8 mol/L.This study further explored the binding ratio and binding constant of colchicine with BSA,and they were 1 and 2.40×105 L/mol.

【基金】 中南大学研究生教育创新工程项目(2010SSXT133)资助
  • 【文献出处】 分析试验室 ,Chinese Journal of Analysis Laboratory , 编辑部邮箱 ,2012年06期
  • 【分类号】R914
  • 【被引频次】8
  • 【下载频次】137
节点文献中: 

本文链接的文献网络图示:

本文的引文网络