1-苯胺基萘-8-磺酸盐、曙红和荧光素与牛血清白蛋白的个体及竞争性结合的荧光探针

Fluorimetric probes of the individual and competitive binding of 1-anilinonaphthalene-8-sulfonate, eosine and fluorescene to bovine serum albumin.

作者信息

Pal M K, Patra S K

机构信息

Department of Biochemistry & Biophysics, University of Kalyani, West Bengal, India.

出版信息

Indian J Biochem Biophys. 1994 Apr;31(2):109-14.

PMID:7523280

Abstract

Fluorescence of 1-anilinonaphthalene-8-sulfonate (ANS) is greatly enhanced on its binding to bovine serum albumin (BSA). Fluorimetric titration shows that three ANS molecules bind per BSA molecule. The enhanced fluorescence of BSA-ANS is quenched by eosine (EOS); and one EOS physically displaces one ANS bound to BSA. The enhanced fluorescence of free ANS in the hydrophobic environment of the nonionic surfactant Triton X 100 is also quenched by EOS but by an energy transfer mechanism. The dye fluorescene (FLSN) also quenches the fluorescence of BSA-bound ANS, but by the energy transfer mechanism. The binding region of ANS in BSA has been speculated.

摘要

1-苯胺基萘-8-磺酸盐（ANS）与牛血清白蛋白（BSA）结合时荧光会显著增强。荧光滴定表明，每个BSA分子结合三个ANS分子。BSA-ANS增强的荧光被曙红（EOS）淬灭；且一个EOS分子会物理取代一个与BSA结合的ANS分子。在非离子表面活性剂Triton X 100的疏水环境中，游离ANS增强的荧光也会被EOS淬灭，但通过能量转移机制。染料荧光素（FLSN）也会淬灭与BSA结合的ANS的荧光，但也是通过能量转移机制。已经推测出ANS在BSA中的结合区域。