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Figure 9.5. Experimental arrangement for paper electrophoresis.
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Figure 9.6. High-voltage paper electrophoresis with cooling.
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high currents involved, heat is generated (as i2 R), and cooling plates are necessary (Fig. 9.6) to maintain constant temperature. An in atable bag is used under the cooling plates for support. The complete resolution of mixtures of amino acids or nucleotides is not always possible after a single high-voltage run. For this reason, 2D techniques are sometimes used, where perpendicular electrophoresis runs or electrophoresis followed by perpendicular chromatography may be used. The careful selection of running buffers and chromatographic eluents allows the resolution of overlapped bands in the second dimension. Cellulose acetate was introduced in 1957 as an alternative to cellulose (paper) as a support material. Cellulose possesses both electrophoretic and chromatographic separation properties, since many components will adsorb onto, or interact with, the hydroxyl groups on the support. Because of this, spots and bands exhibit tailing and resolution is low. Cellulose acetate minimizes the adsorption effect, since most of the hydroxyl groups have been acetylated. Separations using cellulose acetate are more rapid, with improved resolution and less tailing, leading to the facilitated detection of more concentrated spots or bands. In addition, the background staining of cellulose acetate is lower than paper, since stain adsorption is also minimized. Cellulose acetate has two other advantages over paper: it is transparent, facilitating optical detection of zones, and it dissolves easily in a variety of solvents, facilitating the elution and isolation of separated components. 9.2.2. Starch Gels Starch was the rst gel medium used for an electrophoretic separation, and was introduced in 1958. The gel is prepared by heating a paste of potato starch in the electrophoresis buffer until the starch grains burst and the heterogeneous mixture becomes transparent and homogeneous. The hot solution is then poured into a horizontal tank and cooled to ambient temperature, yielding a semisolid gel. As shown in Figure 9.7, a slot is cut into the gel, and sample is introduced as a slurry with starch grains. The surface of the gel is then sealed with wax or grease. Porous wicks are inserted directly into the ends of the gel, and function as electrical connections between the gel and the anodic and cathodic buffer compartments. Following the electrophoretic run, the semisolid gel is removed from the tank, and is cut into layers for staining. This preparative technique allows replicate layers to be stained with different reagents, and leaves macroscopic quantities of unstained
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Figure 9.7. Starch gel electrophoresis.
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material for isolation and further study. The positioning of the sample slot with respect to the anodic and cathodic ends of the gel is based upon an initial knowledge of the species of interest (its isoelectric pH or net charge) or is varied over multiple runs if analyte charge is unknown. The migration of species in the starch gel depends on both the net charge and the molecular size. The gel has a sieving effect, so that small molecules tend to have greater mobilities. The sieving effect can be controlled to some extent through the pore size of the gel, which may be varied by varying the starch concentration; however, the porosity of starch gels may be controlled only over a limited range of concentration, and starch concentrations that are too high or too low yield gels that are excessively stiff or soft. The starch polymer possesses negatively charged side chains (carboxylates) that can interact with proteins and hinder migration by an ion-exchange retention mechanism, so that starch gels, like cellulose, may possess both electrophoretic and chromatographic properties. The negative charge on the gel also leads to a phenomenon called electroosmosis, wherein positively charged counterions (H3O ) in the running buffer move toward the cathode. In effect, the buffer ows toward the cathode, and the overall transport of analyte species in the gel is the sum of transport due to electrophoretic migration and transport due to electroosmosis. The electroosmotic effect can be quantitated using blue dextran, an uncharged oligosaccharide that possesses zero electrophoretic mobility. Blue dextran may be added to a sample, and the migration of the blue dextran from the sample origin is measured after electrophoresis and subtracted from other measured distances to provide corrected migration distances. Starch has been superceded by polyacrylamide and agarose gels for most applications, but is still occasionally used for the separation of isoenzymes. 9.2.3. Polyacrylamide Gels Polyacrylamide gel electrophoresis (PAGE) has replaced starch gel electrophoresis for the separation of proteins, small RNA fragments and very small DNA fragments. Polyacrylamide is more versatile than starch, because the molecular sieving effect can be controlled to a much greater extent, and because the adsorption of proteins to the gel is negligible. Polyacrylamide gels are prepared3 by the reaction of acrylamide (monomer) with N,N 0 -methylenebis(acrylamide) (cross-linker) in the
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