Study on the Action Features between Alvizarin-violet and Bovine Serum Albumin by Fluorescence Spectrophtometry

Under the different temperatures,the binding of alizarin-violet to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy,three-dimension,synchronous fluorescence spectrum and ultra-violet spectrum.After analyzing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,BSA was reacted with Alizarin-Violet and a new compound was found,the quenching belonged to static fluorescence quenching,action force was electro- static interaction each other,the average value of binding constant(KLB:1.078 ×105L·mol-1),thermodynamic parameters(ΔH θ:-8.030kJ·mol-1,ΔGθ:-29.19kJ·mol-1 and ΔSθ:69.80 J·K-1),the binding locality is an area of 2.38 nm away from tryptophan residue-212 in BSA and amounts of binding sites of 1.173 were obtained.It provides important information for reserching the configuration modification of BSA because added lizarin-Violet, and biological effects of Alizarin-Violet and effects of zoology surroundings,and dyeing mechanism for the cells.