Interaction of Carbofuran and Bovine Serum Albumin by Spectrometry

[Objective]The aim was to study the interaction characteristic of bovine serum albumin （BSA） and carbofuran. [ Method]With synchronous fluorescence spectrometry adopted, the interaction of carbofuran and BSA in Tris-HCI buffer system （pH 7.40） was investigated. The binding constants at different tem...

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Bibliographic Details
Published in动物与饲料科学：英文版 Vol. 4; no. 3; pp. 138 - 141
Main Author xu Guang-fu TAN Ya-ya LI Bo
Format Journal Article
LanguageEnglish
Published 2012
Subjects
BSA
克百威
同步荧光光谱法
呋喃丹
牛血清白蛋白
相互作用
结合常数
缓冲系统
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Summary:[Objective]The aim was to study the interaction characteristic of bovine serum albumin （BSA） and carbofuran. [ Method]With synchronous fluorescence spectrometry adopted, the interaction of carbofuran and BSA in Tris-HCI buffer system （pH 7.40） was investigated. The binding constants at different temperatures were calculated and the interaction types between carbofuran and BSA were discussed. [ Result] Under normal physiological conditions, higher quenching effect of carbofuran on BSA was electrostatic interaction. The changes of different drug concentrations and temperature proved a static quenching of carbofuran with BSA. The binding constants （KSV） at 25 ℃, 37 ℃ and 50 ℃ were 1.17 × 10^4, 1.07 × 10^4 and 0. 99 × 10^4 L/mol respectively with ratio of carbofuran and BSA at 1 ： 1. [ Conclusion ] The research is of guiding significance for learning transport and metabolism of carbofuran at molecular level.
Bibliography:[Objective]The aim was to study the interaction characteristic of bovine serum albumin （BSA） and carbofuran. [ Method]With synchronous fluorescence spectrometry adopted, the interaction of carbofuran and BSA in Tris-HCI buffer system （pH 7.40） was investigated. The binding constants at different temperatures were calculated and the interaction types between carbofuran and BSA were discussed. [ Result] Under normal physiological conditions, higher quenching effect of carbofuran on BSA was electrostatic interaction. The changes of different drug concentrations and temperature proved a static quenching of carbofuran with BSA. The binding constants （KSV） at 25 ℃, 37 ℃ and 50 ℃ were 1.17 × 10^4, 1.07 × 10^4 and 0. 99 × 10^4 L/mol respectively with ratio of carbofuran and BSA at 1 ： 1. [ Conclusion ] The research is of guiding significance for learning transport and metabolism of carbofuran at molecular level.
Carbofuran; Bovine serum albumin; Fluorescence spectrometry; Interaction
ISSN:1943-9911