Studies on the interaction between mytomycin C and bovine serum albumin

The binding characteristics of mytomycin C (MMC) with bovine serum albumin (BSA) have been studied by fluorescence spectsoscopy and microcalorimetry m ethod in aqueous solution. The equilibrium constant KA, the number of bindi ng sites n, and the thermodynamic functions for the reaction have all been measured. The binding distance between MMC and BSA and the transfer efficie ncy have been obtained based on the mechanism of Forster energy transfer. T he effect of MMC on the conformation of BSA has also been analyzed using sy nchronous fluorescence spectroscopy.