高等学校化学研究 ›› 2010, Vol. 26 ›› Issue (2): 189-193.
Determination of Protein via Resonance Light Scattering Technique with (NH4)2SO4
WU Li-hang1, MU Dan1, LIANG Fang-hui2, TIAN Yuan1, ZHANG Han-qi1, YU Ai-min1, WANG Xing-hua1* and CHEN Ying3
- 1. College of Chemistry, Jilin University, Changchun 130012, P. R. China;
2. Department of Pharmaceutical Science, Changchun Medical College, Changchun 130031, P. R. China;
3. Jilin Province Center of Environmental Monitoring, Changchun 130011, P. R. China
Determination of Protein via Resonance Light Scattering Technique with (NH4)2SO4
WU Li-hang1, MU Dan1, LIANG Fang-hui2, TIAN Yuan1, ZHANG Han-qi1, YU Ai-min1, WANG Xing-hua1* and CHEN Ying3
- 1. College of Chemistry, Jilin University, Changchun 130012, P. R. China;
2. Department of Pharmaceutical Science, Changchun Medical College, Changchun 130031, P. R. China;
3. Jilin Province Center of Environmental Monitoring, Changchun 130011, P. R. China
摘要：
Be able to form large particles with protein via electrostatic force to enhance the intensity of resonance light scattering(RLS), (NH4)2SO4 was used as a RLS probe to determine bovine serum albumin(BSA), human serum albumin(HSA) and ovum albumin(OVA). The experimental conditions were investigated, including the acidity and saturation degree of (NH4)2SO4. Under the optimum conditions, the enhanced RLS intensity is proportional to the concentration of BSA, HSA and OVA in the ranges of 5×10–8―1×10–6, 2.5×10–8―8×10–7 and 5×10–8―1.5×10–6 mol/L, respectively. The detection limits for BSA, HAS and OVA are 6.6×10–9, 3.8×10–9 and 7.4×10–9 mol/L, respectively. The effects of foreign substances were also examined. The practical and synthetic samples were analyzed with satisfactory results.