乙二胺-N,N′-二邻氨基苯甲酸与牛血清白蛋白作用的荧光光谱研究

Fluorescence Study on the Interaction of Ethylene-N,N'-Dianthranilate and Bovine Serum Albumin

在pH7.4,0.05mol.L-1Tris-HCl条件下,采用荧光光谱法研究了乙二胺-N,N′-二邻氨基苯甲酸(EDA)与牛血清白蛋白(BSA)的相互作用。结果表明,EDA与BSA的结合使蛋白质的荧光被猝灭,条件稳定常数为lgK=5.81±0.04,结合位点数为1,并依据Foerster能量转移理论确定EDA与BSA色氨酸残基的最近距离r为2.14nm。

In 0.05mol · L^-1 Tris-HCl buffer （at pH7. 4）,the interaction between N＇-dianthranilate （EDA） and bovine serum albumin （BSA） was studied by fluorescence ethy and lene-N, UV-Vis absorption spectra. The quenching mechanism of the combination of BSA with EDA is a static quenching procedure, the conditional stability constant and the number of binding sites were determined as lgK= 5.81±0. 04,n= 1, respectively. Meanwhile, the distance between donor （Trp in BSA） and acceptor （EDA） was obtained as r = 2. 14nm based on the theory of Foerster energy transfer.