Study on the resonance Rayleigh scattering and resonance non-linear scattering spectra of ion-association complexes of [PdI4](2-)-protein systems and their analytical applications.

In an acid medium solution, proteins such as bovine serum albumin, human serum albumin, ovalbumin, hemoglobin, lysozyme, gamma-globulin, alpha-chymotrypsin and papain could react with [PdI(4)](2-) by virtue of electrostatic attraction and hydrophobic force to form ion-association complexes. As a result, the resonance Rayleigh scattering (RRS) and resonance nonlinear scattering such as second-order scattering (SOS) and frequency doubling scattering (FDS) intensities were enhanced greatly and new scattering spectra appeared. The maximum scattering peaks of RRS, SOS and FDS were at 367, 720 and 370 nm, respectively.