2013•Chemistry & BioengineeringRequires access

Fluorescence Spectrometric Analysis on the Interaction between L-Cysteine and Bovine Serum Albumin

BI Yu-qi

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Abstract

The interaction between L-cysteine(L-Cys) and bovine serum albumin(BSA) was investigated by fluorescence quenching spectrum and synchronous fluorescence spectrum.The quenching constant,binding constant,binding sites of L-Cys with BSA,and the thermodynamic parameters(△H,△G,△S)were calculated.The fluorescence of BSA was quenched by L-Cys.The fluorescence peak of BSA shifted from 350 nm to 347.5 nm.Its quenching mechanism was a dynamic process.Their interaction force was hydrophobic force.The synchronous fluorescence spectrum showed that L-Cys influenced the microenvironment around BSA.

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What this paper is about

The interaction between L-cysteine(L-Cys) and bovine serum albumin(BSA) was investigated by fluorescence quenching spectrum and synchronous fluorescence spectrum.The quenching constant,binding constant,binding sites of L-Cys with BSA,and the thermodynamic parameters(△H,△G,△S)were calculated.The fluorescence of BSA was quenched by L-Cys.The fluorescence peak of BSA shifted from 350 nm to 347.5 nm.Its quenching mechanism was a dynamic process.Their interaction force was hydrophobic force.The synchronous fluorescence spectrum showed that L-Cys influenced the microenvironment around BSA.

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Available abstract

The interaction between L-cysteine(L-Cys) and bovine serum albumin(BSA) was investigated by fluorescence quenching spectrum and synchronous fluorescence spectrum.The quenching constant,binding constant,binding sites of L-Cys with BSA,and the thermodynamic parameters(△H,△G,△S)were calculated.The fluorescence of BSA was quenched by L-Cys.The fluorescence peak of BSA shifted from 350 nm to 347.5 nm.Its quenching mechanism was a dynamic process.Their interaction force was hydrophobic force.The synchronous fluorescence spectrum showed that L-Cys influenced the microenvironment around BSA.

Key concepts: Chemistry, Bovine serum albumin, Fluorescence, Quenching (fluorescence), Cysteine, Binding constant, Analytical Chemistry (journal), Hydrophobic effect

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