The binding characteristics of mytomycin C (MMC) with bovine serum albumin (BSA) have been studied by fluorescence spectroscopy and microcalorimetry method in aqueous solution. The equilibrium constant K~A, the number of binding sites n, and the thermodynamic functions for the reaction have all been measured. The binding distance between MMC and BSA and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer. the effect of MMC on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy.

Key words: MUTAGENS, SERUM ALBUMIN, CALORIMETRY, THERMODYNAMIC FUNCTION, CONFORMATION