2011Journal of Inner Mongolia UniversityRequires access

Fluorescence Spectrum Characteristics of Complex of Piroxicam,Copper(II) and BSA

Zhihong Zhao

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Abstract

The effects of Piroxicam(PIR),Cu(Ⅱ) on the fluorescence spectrum characteristics of bovine serum albumin(BSA)were studied.The effect of Cu(Ⅱ) on the fluorescence spectrum characteristics of PIR-BSA complex was also investigated.The results showed that both Cu(Ⅱ) and PIR could quench the fluorescence intensity of BSA via a nonradiative energy transfer mechanism.Moreover,when Cu(Ⅱ) was present PIR could more significantly quench the fluorescence of BSA.The binding constants(K) and the binding sites(n) were calculated after analyzing fluorescence quenching data with a double-reciprocal equation.K and n between PIR and BSA were 3.18×103L/mol and 0.75 respectively in the PIR-BSA complex,while that between Cu(Ⅱ) and BSA were 1.13×103 L/mol and 0.74 respectively in the binary complex of copper(Ⅱ) and BSA.

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What this paper is about

The effects of Piroxicam(PIR),Cu(Ⅱ) on the fluorescence spectrum characteristics of bovine serum albumin(BSA)were studied.The effect of Cu(Ⅱ) on the fluorescence spectrum characteristics of PIR-BSA complex was also investigated.The results showed that both Cu(Ⅱ) and PIR could quench the fluorescence intensity of BSA via a nonradiative energy transfer mechanism.Moreover,when Cu(Ⅱ) was present PIR could more significantly quench the fluorescence of BSA.The binding constants(K) and the binding sites(n) were calculated after analyzing fluorescence quenching data with a double-reciprocal equation.K and n between PIR and BSA were 3.18×103L/mol and 0.75 respectively in the PIR-BSA complex,while that between Cu(Ⅱ) and BSA were 1.13×103 L/mol and 0.74 respectively in the binary complex of copper(Ⅱ) and BSA.

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Available abstract

The effects of Piroxicam(PIR),Cu(Ⅱ) on the fluorescence spectrum characteristics of bovine serum albumin(BSA)were studied.The effect of Cu(Ⅱ) on the fluorescence spectrum characteristics of PIR-BSA complex was also investigated.The results showed that both Cu(Ⅱ) and PIR could quench the fluorescence intensity of BSA via a nonradiative energy transfer mechanism.Moreover,when Cu(Ⅱ) was present PIR could more significantly quench the fluorescence of BSA.The binding constants(K) and the binding sites(n) were calculated after analyzing fluorescence quenching data with a double-reciprocal equation.K and n between PIR and BSA were 3.18×103L/mol and 0.75 respectively in the PIR-BSA complex,while that between Cu(Ⅱ) and BSA were 1.13×103 L/mol and 0.74 respectively in the binary complex of copper(Ⅱ) and BSA.

Key concepts: Bovine serum albumin, Fluorescence, Quenching (fluorescence), Copper, Chemistry, Analytical Chemistry (journal), Piroxicam, Nuclear chemistry

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