What method utilizes gels to determine the purity of a protein sample?

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Electrophoresis is the method that utilizes gels to determine the purity of a protein sample. This technique separates proteins based on their size and charge as they migrate through a gel matrix under an electric field. By applying an electric current, the proteins move through the gel, with smaller proteins traveling faster and further than larger ones. After running the gel, the resulting bands can be visualized, allowing for the assessment of the purity of the protein sample. If a sample contains multiple proteins, they will appear as distinct bands, helping to identify contaminants or verify the presence of a specific protein.

Other methods mentioned serve different purposes. Chromatography separates molecules based on their chemical properties but typically does not utilize gels; it focuses on liquid or solid phases. Western blotting involves transferring proteins from a gel to a membrane for detection using antibodies, which is a step after electrophoresis, not a method of assessing purity directly. Enzyme-linked immunosorbent assay (ELISA) is used for quantifying proteins or hormones using antibodies but does not provide information on purity through gel separation.