Abstract
The interaction of benzidine (BEN) with trypsin was studied by fluorescence spectrum. It was shown that BEN has quenched the fluorescence launching from trypsin by reacting with it and forming a certain kind of new complex. The quenching and energy transfer mechanisms were discussed. The binding constants and thermodynamic parameters at three different temperatures, the binding locality, and the binding power were obtained. The conformation of trypsin was discussed by synchronous and three-dimensional fluorescence techniques.
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