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- W2373847576 abstract "The interaction characteristic of labetalol and bovine serum albumin(BSA) was investigated by fluorescence spectrometry and ultra-violet absorption spectrometry.The results show that the quenching mechanism of the intrinsic fluorescence of BSA by labetalol is a static quenching procedure in the weak acid medium,while that is kinetic quenching procedure in the weak basic or neutral medium.The binding site is a distance 2.74 nm away from BSA based on Frster snon-radiation energy transfer mechanism.The thermodynamic parameters show that the binding foroce between labetalol and BSA is mainly the hydrophobic interaction.Synchronous spectrum was used to investigate the conformational change of BSA.In addition,the common ions also influence the binding of labetalol to BSA." @default.
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- W2373847576 date "2011-01-01" @default.
- W2373847576 modified "2023-09-25" @default.
- W2373847576 title "Study on the interaction of labetalol and bovine serum albumin by fluorescence spectrometry" @default.
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