Fluorescence spectrometric study on the interactions of Isoprocarb and sodium 2-isopropylphenate with bovine serum albumin.
作者： Yongnian Ni , Genlan Liu , Serge Kokot
DOI: 10.1016/J.TALANTA.2008.03.037
关键词:
摘要: The binding interaction of the pesticide Isoprocarb and its degradation product, sodium 2-isopropylphenate, with bovine serum albumin (BSA) was studied by spectrofluorimetry under simulated physiological conditions. Both 2-isopropylphenate quenched intrinsic fluorescence BSA. This quenching proceeded via a static mechanism. thermodynamic parameters (ΔH°, ΔS° ΔG°) obtained from data measured at two different temperatures showed that to BSA involved hydrogen bonds hydrophobic electrostatic interactions. Synchronous spectroscopy either or molecular structure changed significantly, which is consistent known toxicity pesticide, i.e., protein denatured. estimated be about 4–5 times more toxic than parent, Isoprocarb. Synchronous resolution three-way excitation–emission spectra PARAFAC method extracted relative concentration profiles BSA, Isoprocab as function added 2-isopropylphenate. These displaced in competitive reaction protein.
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