Sodium sodecylsulfate polyacrylamide gel electrophoresis is a technique that separates protein on the basis of molecular weight. The gel porosity can be controlled through regulating the cross-linking extent. As the acrylamide concentration increases, the gel porosity decreases and any protein molecule migrates more slowly after application of the same electrical current. Presence of SDS detergent in the gel disrupts the non-covalent bonds of proteins and coats the polypeptides resulting to a net negative charge. Reducing agent Î²-mercaptoethanol addition disrupts the disulfide bridges present in the protein. The larger protein moves slower than small molecules in the polyacrylamide gel. The approximate size of the protein estimation is by running a protein molecular weight marker along the samples.
A standard curve can generation can be done using the standard proteins of known molecular weight. A plotted graph with the distance of migration versus molecular weight can be used to estimate the molecular weight of unknown protein. The unknown protein is electrophoresed parallel to the standard molecular weight samples. The resolution of SDS-PAGE can be increased by using two polyacrylamide gel layers having different levels of cross-linking. The upper gel (stacking gel) contains a lesser degree of cross-linking, making polypeptides move fast in this layer. The running gel (lower gel) contains a higher degree of cross-linking and polypeptides move slowly in this layer. The slowing down of the speed of movement results to all polypeptides piling up and get condensed to a tight band that enters the running gel. A polyacrylamide gradient use such that the polyacrylamide percentage increases downwards also increases protein resolution. This allows protein separation into a greater range of molecular weights than the use of uniform concentration of acrylamide throughout the gel.
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