2010Journal of Nanchang UniversityRequires access

Interaction Between Dobutrex and Bovine Serum Album by Fluorescent Spectra

NI Yong-niana

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Abstract

The interaction between dobutrex and bovine serum albumin(BSA) was studied by fluorescence spectra under the simulated physiological condition.It was shown that this compound has a quite strong ability to quench the intrinsic fluorescence of BSA.The quenching mechanism was static quenching procedure.The fluorescence quenching data were analyzed according to Stern – Volmer equation and Line weaver-Burk equation,thermodynamic parameters,binding constants Ka,the number of binding sites n were evaluated at 298,301 and 304 K,respectively.The main sorts of acting force between the drug and BSA was found to be hydrophobic force.The site markers competitive experiments indicated that the binding of dobutrex and bovine serum albumin primarily in site II.The effect of dobutrex on the conformation of BSA was analyzed by synchronous fluorescence.

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What this paper is about

The interaction between dobutrex and bovine serum albumin(BSA) was studied by fluorescence spectra under the simulated physiological condition.It was shown that this compound has a quite strong ability to quench the intrinsic fluorescence of BSA.The quenching mechanism was static quenching procedure.The fluorescence quenching data were analyzed according to Stern – Volmer equation and Line weaver-Burk equation,thermodynamic parameters,binding constants Ka,the number of binding sites n were evaluated at 298,301 and 304 K,respectively.The main sorts of acting force between the drug and BSA was found to be hydrophobic force.The site markers competitive experiments indicated that the binding of dobutrex and bovine serum albumin primarily in site II.The effect of dobutrex on the conformation of BSA was analyzed by synchronous fluorescence.

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Available abstract

The interaction between dobutrex and bovine serum albumin(BSA) was studied by fluorescence spectra under the simulated physiological condition.It was shown that this compound has a quite strong ability to quench the intrinsic fluorescence of BSA.The quenching mechanism was static quenching procedure.The fluorescence quenching data were analyzed according to Stern – Volmer equation and Line weaver-Burk equation,thermodynamic parameters,binding constants Ka,the number of binding sites n were evaluated at 298,301 and 304 K,respectively.The main sorts of acting force between the drug and BSA was found to be hydrophobic force.The site markers competitive experiments indicated that the binding of dobutrex and bovine serum albumin primarily in site II.The effect of dobutrex on the conformation of BSA was analyzed by synchronous fluorescence.

Key concepts: Bovine serum albumin, Quenching (fluorescence), Fluorescence, Chemistry, Analytical Chemistry (journal), Chromatography, Physics, Quantum mechanics

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