Determination of protein by resonance light scattering technique using dithiothreitol-sodium dodecylbenzene sulphonate as probe.

The resonance light scattering (RLS) spectra of bovine serum albumin (BSA)-dithiothreitol (DTT)-sodium dodecylbenzene sulphonate (SDBS) and its analytical application were investigated. The RLS intensity of this system can be effectively enhanced in the presence of BSA. Based on the enhanced RLS intensity, a simple assay for BSA was developed. The experimental results indicate that the enhanced RLS intensity is proportional to the concentration of BSA in the range from 1.0 x 10(-8) to 7.5 x 10(-7) mol L(-1) with the determination limit of 5.0 x 10(-9) mol L(-1). The effects of pH, concentration of SDBS and DTT on the RLS enhancement were discussed. Most metal ions have little interference on the determination of BSA. Some synthetic and real samples were analyzed, and the results obtained were in good agreement with those obtained by Bradford method.