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酞菁铁Ⅱ与牛血清白蛋白相互作用的光谱研究
引用本文:钟平,刘海东.酞菁铁Ⅱ与牛血清白蛋白相互作用的光谱研究[J].赣南师范学院学报,2014(6):35-37.
作者姓名:钟平  刘海东
作者单位:赣南师范学院化学化工学院,江西赣州,341000
摘    要:研究酞菁铁Ⅱ与牛血清白蛋白的相互作用,测定了二者相互作用的荧光光谱和紫外可见光谱.荧光光谱分析表明,随着酞菁铁Ⅱ浓度的增加,后者在345 nm处荧光有规律的发生猝灭现象.根据Stern-Vo Lmer方程可以计算得到两者相互作用的猝灭常数为1.25×104,结合位点数为1.由紫外可见光谱可知,随着酞菁铁Ⅱ浓度的增加,牛血清白蛋白在210 nm处吸光度有所上升,峰位发生红移.

关 键 词:酞菁铁Ⅱ  牛血清白蛋白  光谱研究

The Spectrum Research on the Interaction of Iron Phthalocyanine II and Bovine Serum Albumin
ZHONG Ping,LIU Haidong.The Spectrum Research on the Interaction of Iron Phthalocyanine II and Bovine Serum Albumin[J].Journal of Gannan Teachers' College(Social Science(2)),2014(6):35-37.
Authors:ZHONG Ping  LIU Haidong
Institution:(School of Chemistry and Chemical Engineering, GanNan Normal University, Ganzhou 341000, China)
Abstract:The fluorescence spectrum and UV-visible spectrum are tested by the interaction of Iron Phthalocyanine II and Bovine Serum Albumin. The fluorescence spectrum shows that with the increase of the density of Iron Phthalocyanine, the latterg fluorescence quenches regularly at 345 nm. Calculating by the Stern-VoLmer equation, the quenching constant of the interaction is 1.25 × 10, and the number of binding sites is 1. UV-visible spectrum shows that with the increase of the density of Iron Phthalocyanine, Bovine Serum Albumin g absorbance increases at 210nm, it' peak position red shifts.
Keywords:iron phthalocyanine II  bovine serum albumin  spectrum research
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