2010•Journal of Hainan Normal UniversityRequires access

Study on the Interactions Between Theophylline and Bovine Serum Albumins by Fluorescence Spectroscopy

Yanli Wei

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Abstract

The interactions between Theophylline and bovine serum albumin(BSA) were studied by fluorescence and UV absorption spectroscopy.The binding constants KA(1.96×104,3.80×104,1.57×105) and binding sites n(1.0,1.1,1.2) were measured at different temperatures of 10 ℃,28 ℃ and 40 ℃.The results revealed that Theophylline has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as static quenching procedure.According themodynamic parameters the acting forces were determined to be hydrophobic force.

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The interactions between Theophylline and bovine serum albumin(BSA) were studied by fluorescence and UV absorption spectroscopy.The binding constants KA(1.96×104,3.80×104,1.57×105) and binding sites n(1.0,1.1,1.2) were measured at different temperatures of 10 ℃,28 ℃ and 40 ℃.The results revealed that Theophylline has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as static quenching procedure.According themodynamic parameters the acting forces were determined to be hydrophobic force.

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Available abstract

The interactions between Theophylline and bovine serum albumin(BSA) were studied by fluorescence and UV absorption spectroscopy.The binding constants KA(1.96×104,3.80×104,1.57×105) and binding sites n(1.0,1.1,1.2) were measured at different temperatures of 10 ℃,28 ℃ and 40 ℃.The results revealed that Theophylline has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as static quenching procedure.According themodynamic parameters the acting forces were determined to be hydrophobic force.

Key concepts: Theophylline, Bovine serum albumin, Chemistry, Fluorescence spectroscopy, Quenching (fluorescence), Fluorescence, Spectroscopy, Absorption (acoustics)

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