Abstract
Electrophoresis is capable of resolving biological materials on the basis of differences in their molecular weights, electrophoretic mobilities, isoelectric points, or various combinations of these properties. At laboratory scale, these include some of the most powerful techniques available for the gentle purification of biologically active molecules. For instance, isoelectric focusing (IEF, see Table 1) can resolve proteins whose isoelectric points, pIs, differ by as little as 0.01 pH unit. Likewise, SDS-PAGE will routinely isolate a discrete spectrum of proteins whose molecular weights differ by less than 2%. Although electrophoretic separations are sometimes carried out under hostile conditions, e.g., low salt concentrations, denaturing detergents, or extreme pHs, the basic technique is inherently mild and is universally applicable to the detection and purification of solutes ranging in size from several ångströms to several microns. Because of this, electrophoresis is widely used in the natural sciences for both analytical and prepative work.

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