By using the techniques of resonance light scattering (RLS) and absorption spectra, we studied the toxicosis and detoxifcation mechanism of anionic surfactant SDBS and cationic surfactant CTMAB targeted to bovine serum albumin (BSA). Small quantity of CTMAB combines with SDBS-BSA complex to form SDBS-BSA-CTMAB complex and the IRLS of system enhanced greatly. With the cumulation of quantity, CTMAB captures SDBS from SDBS-BSA complex by electrostatic attraction and CTMAB-SDBS complex forms, meanwhile BSA automatically frees, which is corresponding to the toxicosis and detoxifcation process. Absorption experiment validates that SDBS induces the denaturalization of BSA and CTMAB facilitates the refolding of this protein.