Investigation of the interaction between acridine orange and bovine serum albumin

被引：386

作者：

Feng, XZ ^{[1
]}

Lin, Z ^{[1
]}

Yang, LJ ^{[1
]}

Wang, C ^{[1
]}

Bai, CL ^{[1
]}

机构：

[1] Acad Sinica, Inst Chem, Beijing 100080, Peoples R China

来源：

TALANTA | 1998年 / 47卷 / 05期

基金：

中国国家自然科学基金;

关键词：

acridine orange; bovine serum albumin; equilibrium constant; binding sites; energy transfer;

D O I：

10.1016/S0039-9140(98)00198-2

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The results from the measurement of the fluorescence spectrum showing the binding characteristics of acridine orange (AO) and bovine serum albumin (BSA) are reported. It was found that the equilibrium constant k = 4848.64 1 mol(-1), and the number of binding sites n = 0.82. Based on the mechanism of the Forster energy transference, the transfer efficiency of energy and distance between the acceptor AO and BSA were found. The interaction between AO and BSA have been verified as consistent with the static quenching procedure and the quenching mechanism is related to the energy transfer. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：1223 / 1229

页数：7

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