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Updated: Jun 29, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
Published on: April 1, 2017
[Resonance scattering spectra of apolipoprotein immunocomplex particles and its analytical application]
Shuang-Jiao Sun1, Ai-Hui Liang, Zhi-Liang Jiang
1School of Environment and Resource, Guangxi Normal University, Guilin 541004, China.
Abstract:
In pH 6.8 Na2 HPO4-NaH2PO4 buffer solution and in presence of polyethylene glycol (PEG), apolipoprotein AI (ApoAI) and apolipoprotein B (ApoB) would combine with their corresponding antibody and produced immune complex particles in size of about 180 nm and 140 nm respectively, which exhibit stronger resonance scattering (RS) effect at 340 nm and 470 nm. The influence of pH, antisera volume, PEG concentration, incubation time and co-exists substances was considered. Under the optimal conditions, the RS intensity is proportional to the concentrations of ApoAI and ApoB when their concentration is in the range of 8.4-430.0 ng x mL(-1) and 14.8-590.0 ng x mL(-1), respectively. The detection limits (DL) are 6.2 ng x mL(-1) for ApoAI and 7.0 ng x mL(-1) for ApoB. The method was successfully applied to determination of ApoAI and ApoB in human serum samples, with satisfactory results.
