Abstract
Strong evidence has been accumulated from our recent small-angle neutron-scattering and phase-separation studies to support the view that protein--sodium-dodecylsulfate (SDS) complexes in solution are polymerlike objects. This conclusion is also consistent with the viscosimetric measurements of Reynolds and Tanford, if we we further assume that the protein-SDS complex is a free-draining perturbed polymer. We propose here a reptation mechanism for the explanation of the migration of the protein-SDS complex in polyacrylamide gel during electrophoresis. Electrophoretic data taken from independent experiments have been analyzed to confirm our conjecture.
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