[Study on the spectra of Cal-Red-Cu(II) complex with bovine serum albumin and its analytical application].

The Resonance light scattering (RLS) spectra, fluorescence spectra, and absorption spectra of Cal-Red-Cu(II) metal complex with bovine serum albumin (BSA) were studied. As the Cal-Red-Cu(II)-BSA complex formed, the RLS spectra and fluorescence spectra enhanced, but the absorption spectra weakened and the absorption peak at 594 nm disappeared. At pH 5.65-5.75, the enhanced RLS of Cal-Red-Cu(II) metal complex with BSA system was characterized by the maximum scattering at 317 nm, and the RLS intensity is proportional to the concentration of BSA. Under optimal conditions, the linear range of calibration was 0.75-10 microg x mL(-1), the linear regression equation was I=150. 88+201.48c(BSA, microg x mL(-1))with r=0.9973, and the limit of detection was 5.62 x 10(-2) microg x mL(-1). The method was applied to the determination of BSA in synthetic samples satisfactorily. A mechanism of electrostatic force was suggested for the interaction between BSA and Cal-Red-Cu(II).

[Reaction of atrazine with protein and its application to detection of protein].

The resonance light scattering (RLS) technique and UV-Vis absorption spectra were applied to the investigation of the interaction between atrazine and bovine serum albumin(BSA). Under acidic conditions, the formation of atrazine-BSA supermolecule by Van der Waals force and N/O--H...pi hydrogen bonds leads to a red shift of absorption band and strong RLS enhancement of atrazine. The characteristics and intensity of RLS were related to the pH, the concentration of atrazine, and temperature. Under the optimum conditions, the enhanced RLS intensities are in proportion to the concentration of BSA in the range of 0.05-100 microg x mL(-1). Based on the enhancement of the RLS, a simple and sensitive method for the determination of BSA was established. The detection limit (3sigma) is 12 ng x mL(-1). Synthesis samples were determined with satisfactory results.