胡珍珠, 杨冬冬. 四(邻-氯乙酰胺基)苯基卟啉与牛血清白蛋白的相互作用[J]. 信阳师范学院学报(自然科学版), 2010, 23(1): 68-71.
引用本文: 胡珍珠, 杨冬冬. 四(邻-氯乙酰胺基)苯基卟啉与牛血清白蛋白的相互作用[J]. 信阳师范学院学报(自然科学版), 2010, 23(1): 68-71.
Study on the Interaction between BSA and Tetra(o-chloroacetamide)phenylporphyrin[J]. Journal of Xinyang Normal University (Natural Science Edition), 2010, 23(1): 68-71.
Citation: Study on the Interaction between BSA and Tetra(o-chloroacetamide)phenylporphyrin[J]. Journal of Xinyang Normal University (Natural Science Edition), 2010, 23(1): 68-71.

四(邻-氯乙酰胺基)苯基卟啉与牛血清白蛋白的相互作用

Study on the Interaction between BSA and Tetra(o-chloroacetamide)phenylporphyrin

  • 摘要: 采用荧光光谱法研究四(邻-氯乙酰胺基)苯基卟啉(H2TClPP)与牛血清白蛋白(BSA)的结合作用.通过不同温度下卟啉对BSA作用引起的荧光强度变化,利用荧光猝灭的Stern-Volmer曲线和静态猝灭公式线性拟合,求得反应的结合常数、热力学参数和分子间作用力的类型,证实了H2TClPP对BSA有较强的猝灭能力,其荧光猝灭作用属于静态猝灭.H2TClPP对BSA的同步荧光光谱表明,相互作用使BSA的构象发生了变化.

     

    Abstract: The binding characteristics of BSA and H2TClPP were studied by fluorescence spectroscopy and synchronous fluorescence spectroscopy.The fluorescence intensity of BSA at 341 nm was quenched when H2TClPP was added.The binding site number and binding constant were analyzed at different temperature using Stern-Volmer equation and double-reciprocal equation.The results indicate that BSA can strongly bind H2TClPP with molar ratio of 1∶1,the van der Waals force and hydrogen bond were the main binding force and the quenching was static.Synchronous fluorescence spectroscopy showed that the interaction caused the conformational change of BSA.

     

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