A reducing gel will have beta mercaptoethanol (BME) and/or DTT added to the sample before boiling, and will break any disulfide bonds in the protein. This can result in a protein with quaternary structure (multiple subunits) to yield as many bands as there are subunits in the protein. Non-reducing conditions (no BME) will not break S-S bonds.
A SDS-PAGE will denature the protein, but denaturation is not the same as breaking S-S bonds. A reducing SDS gel will do both (denature and break disulfide bonds).
A reducing gel will have beta mercaptoethanol (BME) and/or DTT added to the sample before boiling, and will break any disulfide bonds in the protein. This can result in a protein with quaternary structure (multiple subunits) to yield as many bands as there are subunits in the protein. Non-reducing conditions (no BME) will not break S-S bonds.
A SDS-PAGE will denature the protein, but denaturation is not the same as breaking S-S bonds. A reducing SDS gel will do both (denature and break disulfide bonds).
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