Abstract
A new, improved method is described, which takes advantage of the low solubility of potassium dodecyl sulfate (KDS), to concentrate sodium dodecyl sulfate-solubilized proteins from nanomolar solutions by KDS precipitation. The method was applied to proteins differing in Mr and pI. The effect of varying KCl, and the pH and/or concentration of the buffer on KDS-protein precipitation was studied. These parameters may be chosen to allow selective repartition of specific proteins in the pellet or supernatant. After precipitation, the hundred- or thousand-fold concentrated solutes are easily resuspended in small volumes of any required medium. Though initially experimented to recover muscle proteins from effluents of electroendosmotic preparative gel electrophoresis, the method proved to be of general interest as a powerful tool to recover proteins from highly diluted solutions.
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