Abstract
Abstract The interaction of sodium dodecyl sulfate (SDS) with the pig serum low-density lipoprotein (LDL) showed a subtle dependence on the SDS concentration. At the SDS concentrations below 0.01%, the binding isotherm conformed to the Langmuir’s type, from which the maximum number of the binding site and the intrinsic binding constant were respectively estimated to be 1600 mol mol−1 and 6.5×103 (mol dm−3)−1. At the SDS concentrations at or above 0.03%, the LDL structure irreversibly dissociated.
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