Electrophoresis (three main methods)

Electrophoresis is a technique used to separate charged molecules, such as proteins and nucleic acids, based on their size and charge. This process occurs in an inert support medium like paper, cellulose acetate, agarose gel, or polyacrylamide gel. When an electric current is applied, the molecules migrate toward their respective electrodes at different speeds, forming distinct zones. These zones can be visualized through staining or detected using analytical methods to determine the composition and concentration of the sample. The first method involves paper electrophoresis. The setup includes an electrophoresis chamber and a DC power supply. The buffer solution used is citrate buffer (pH 3.0). Filter paper is pre-treated by soaking in formic acid overnight, then rinsed and dried. Sample spots are applied either via wet or dry point methods. After electrophoresis, the filter paper is dried and examined under UV light. The bands are cut out and analyzed for content using spectrophotometry. The second method uses cellulose acetate film. The film is soaked in barbiturate buffer (pH 8.6) before spotting. Electrophoresis is performed at a controlled voltage gradient. After migration, the film is stained with amino black and scanned for protein quantification. The relative content of each protein component is determined using elution or scanning techniques. The third method is SDS-polyacrylamide gel electrophoresis (SDS-PAGE), which separates proteins based on molecular weight. SDS binds to proteins, giving them a uniform negative charge. This eliminates the effect of intrinsic charge differences. The gel is prepared using acrylamide and buffers, and samples are loaded into wells. After electrophoresis, the gel is stained with Coomassie blue or silver stain. The migration distance of proteins is measured, and molecular weights are estimated using standard curves. Purity is assessed by analyzing peak areas with a scanner. Each method requires careful preparation of reagents, precise control of electrophoretic conditions, and accurate detection of results. These techniques are widely used in biochemistry and molecular biology for analyzing protein composition, purity, and molecular weight. Proper execution ensures reliable and reproducible data for research and quality control purposes.

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