Polarized synchronous light scattering characterization of the interaction of proteins with sodium d

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In acid buffer solution, proteins with positive charge can react with anion surfactant and result in a great enhancement of synchronous light scattering (SLS) signals. In this contribution, the correlative experiment was made to compare the interaction of human serum albumin (HSA) and immunoglobulin G (IgG) with sodium dodecyl sulfonate (SDS). Based on the measurements of the polarization light scattering signals, a new method of scattering polarization was constituted to distinguish these two interaction systems with molecular weight difference (HSA 66 kDa; IgG 150 kDa). The results were con- sistent with the data measured by dynamic light scattering (DLS) technique. In this buffer, proteins with positive charge can react with anion surfactant and result in a great enhancement of synchronous light scattering (SLS) signals. In this contribution, the correlative experiment was made to compare the interaction of human serum albumin (HSA) and immunoglobulin G (IgG) with sodium dodecyl sulfonate (SDS). Based on the measurements of the polarization light scattering signals, a new method of scattering polarization was constituted to distinguish these two interaction systems with molecular weight difference (HSA 66 kDa; IgG 150 kDa The results were con- stant with the data measured by dynamic light scattering (DLS) technique.
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