The Interaction between Acridine Orange and Bovine Serum Albumin
Feng Xizeng, Bai Chunli, Lin Zhang, Wang Naixin, Wang Chen (Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080)
We report the results on the binding characteristics of acridine orange (AO) and bovine serum albumin (BSA) by measuring fluorescence spectra. The equilibrium constant k was found to be 4. 8 ×103 L/mol, and the number of binding sites n=0. 82. Based on the mechanism of Forster energy transfer, the transfer efficiency of energy and distance between acceptor AO and BSA were obtained. The interaction between AO and BSA have been veri- fied as consistent with static quenching procedure and the quenching mechanism is related to the energy transfer.
【CateGory Index】：
O657.3
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