Abstract
As a resonance light scattering (RLS) probe, the polyelectrolyte polymethacrylic acid (PMAA) was applied in this assay. The bovine serum albumin (BSA) and human serum albumin (HSA) were determined by the electrostatic interaction of PMAA and proteins. At pH 3.8 Na 2HPO 4–citric acid buffer solution, the RLS intensities of PMAA–BSA (HSA) system were greatly enhanced. The characteristic peaks were appeared at the wavelength 320, 546 and 594 nm. The optimization conditions of the reaction were also examined and selected. Under the selected conditions, the RLS intensities were proportional to the protein concentrations in the range of (0.0200–2.00) × 10 −6 mol/L for BSA and (0.0200–2.40) × 10 −6 mol/L for HSA. The influences of some foreign substances were also examined. The synthetic samples containing proteins and some real samples were analyzed and the results obtained were satisfactory.
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