Guang Pu Xue Yu Guang Pu Fen Xi
June 2008
Guang Pu Xue Yu Guang Pu Fen Xi
August 2006
In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the Forster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.
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