In the Phosphate Buffer Saline buffer solution at PH 7.4,the fluorescence quenching characteristics of Bovine Serum Albumin when Ebastine existed were studied by Fluorescence spectra. After experiments,three quenching spectral curve groups were obtained under corresponding temperatures (298K,305K,312K). According to the Stern-Volmer equation,the quenching constants were calculated and then it was concluded: the quenching was belonged to static quenching mechanism. By calculating the thermodynamic parameters of the Ebastine-Bovine Serum Albumin system,it was shown that the binding power between Bovine Serum Albumin and Ebastine was mainly the hydrophobic force. By fitting the double logarithmic equation,the binding constants KA between Bovine Serum Albumin and Ebastine at three temperatures were obtained to be 3.27×104 L·mol－,4.11×104 L·mol－ and 7.59×104 L·mol－,respectively. The number of binding sites were 0.98,1.02,1.08. The binding distance between the donor (Bovine Serum Albumin) and the acceptor (Ebastine) was determined based on the Frster′s non-radiation energy transfer theory and it turned out to be 2.8 nm. The effect of Ebastine on the conformation of Bovine Serum Albumin was analysed by synchronous fluorescence spectra and three-dimensional fluorescence spectra.