Citation:
CHI Yan-Hua, ZHUANG Jia, BI Xin-Ying, ZHOU Lei. Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method[J]. Chinese Journal of Applied Chemistry,
;2007, 24(10): 1167-1171.
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The interaction mechanism of diethylmalonylurea(BBT) with bovine serum albumin(BSA) was studied by fluorescence and UV-Vis spectra. It is shown that BBT has a powerful ability to quench the fluorescence intensity of BSA. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation at 17℃ and 37℃ to obtain the quenching constants, 17℃KSV=1.427×104 and 37℃KSV=1.195×104, 17℃KLB=9.848×103 and 37℃KLB=1.778×103, and the binding constant K0=4.341×104, and the thermodynamic parameters(ΔH, ΔS and ΔG). It was deduced that combining site n was 1.136. The increasing of temperature was favorable for the BBT-BSA interaction. According to the thermodynamic parameters, the major binding forces were determined. The effect of BBT on the conformation of BSA was analyzed Via synchronous fluorescence spectroscopy.
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