Binding Constants for Terbium(Ⅲ) with Chicken Apoovotransferrin  

作　　者：YANG Bin sheng LI Ying qi 

机构地区：[1]Institute of Molecular Science,Shanxi University,Taiyuan 030006,P.R.China

出　　处：《Chemical Research in Chinese Universities》2001年第1期6-13,共8页高等学校化学研究(英文版)

基　　金：SupportedbytheNationalNaturalScienceFoundationofChina(No .2 0 0 710 2 2 0 ) ;NaturalScienceFoundationofShanxiProvince(No .9910 13)andShanxiReturned scholarFoundation

摘　　要：The binding of Tb 3+ to chicken apoovotransferrin was studied by monitoring the fluorescent intensity of Tb 3+ at 549 nm. The conditional equilibrium constants for the complexation of Tb 3+ by chicken apoovotransferrin in 0 1 mol/L hepes, at pH 7 4 and room temperature were measured. The successive macroscopic binding constants are lg K 1=9 08±0 12 and lg K 2=7 36±0 22. The molar fluorescence enhancement of Tb 3+ apoovotransferrin complex is (2 06±0 14)×10 4 mol -1 ·L. The fluorescence quenching experiment and the titration of N terminal monoferric ovotransferrin showed that Tb 3+ has a preference for being bound to the N terminal binding site of apoovotransferrin.The binding of Tb 3+ to chicken apoovotransferrin was studied by monitoring the fluorescent intensity of Tb 3+ at 549 nm. The conditional equilibrium constants for the complexation of Tb 3+ by chicken apoovotransferrin in 0 1 mol/L hepes, at pH 7 4 and room temperature were measured. The successive macroscopic binding constants are lg K 1=9 08±0 12 and lg K 2=7 36±0 22. The molar fluorescence enhancement of Tb 3+ apoovotransferrin complex is (2 06±0 14)×10 4 mol -1 ·L. The fluorescence quenching experiment and the titration of N terminal monoferric ovotransferrin showed that Tb 3+ has a preference for being bound to the N terminal binding site of apoovotransferrin.

关 键 词：TERBIUM TRANSFERRIN Binding constant FLUORESCENCE 

分 类 号：O614[理学—无机化学]