2009Chinese Journal of Spectroscopy LaboratoryRequires access

Studies on the Interaction Between Evansblue and Bovine Serum Albumin by Fluorescence Spectrophotometry

Li Ma

Open publisher page 0 citations

Abstract

The interaction of evansblue(EB) and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and ultraviolet spectroscopy.The experimental results showed that EB could quench the inner fluorescence of BSA by forming the BSA-EB complex.It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching.The binding constants(K)between EB and BSA were 1.122×106L·mol-1,and the binding sites(n) were 0.994.According to Foerster theory of non-radiation energy transfer the binding distance(r=3.14nm) and the efficiency of energy transfer(E=0.276) were also obtained.The effect of EB on the conformational change of BSA was also analyzed by synchronous fluorescence spectroscopy.

About this research paper

What this paper is about

The interaction of evansblue(EB) and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and ultraviolet spectroscopy.The experimental results showed that EB could quench the inner fluorescence of BSA by forming the BSA-EB complex.It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching.The binding constants(K)between EB and BSA were 1.122×106L·mol-1,and the binding sites(n) were 0.994.According to Foerster theory of non-radiation energy transfer the binding distance(r=3.14nm) and the efficiency of energy transfer(E=0.276) were also obtained.The effect of EB on the conformational change of BSA was also analyzed by synchronous fluorescence spectroscopy.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The interaction of evansblue(EB) and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and ultraviolet spectroscopy.The experimental results showed that EB could quench the inner fluorescence of BSA by forming the BSA-EB complex.It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching.The binding constants(K)between EB and BSA were 1.122×106L·mol-1,and the binding sites(n) were 0.994.According to Foerster theory of non-radiation energy transfer the binding distance(r=3.14nm) and the efficiency of energy transfer(E=0.276) were also obtained.The effect of EB on the conformational change of BSA was also analyzed by synchronous fluorescence spectroscopy.

Key concepts: Bovine serum albumin, Fluorescence, Chemistry, Quenching (fluorescence), Fluorescence spectroscopy, Spectroscopy, Ultraviolet visible spectroscopy, Analytical Chemistry (journal)

Related papers

Back to paper searchBrowse research topicsOriginal source
Studies on the Interaction Between Evansblue and Bovine Serum Albumin by Fluorescence Spectrophotometry — Research Paper | ScholarLens