Abstract：The binding feature of pizotifeunm to Bovine Serum Albumin (BSA) was studied using fluorescence spectroscopy. It was shown that this compound had a powerful ability to quench the BSA fluorescence via a nonradiative energy transfer mechanism. The fluorescence quenching data was analyzed according to Scatchard equation and double-reciprocal equation,and the binding constant,and the thermodynamic parameters, etc. were obtained.
收稿日期: 2002-03-25
引用本文:
易长海,颜承农,上官云凤,刘义,潘祖亭,屈松生. 苯噻啶与蛋白质作用特征的热力学研究[J]. , 2002, 41(3): 0-0.
易长海,颜承农,上官云凤,刘义,潘祖亭,屈松生. Studies on the thermodynamics of the binding reaction of pizotifeunm to Bovine Serum Albumin. , 2002, 41(3): 0-0.
