4.2.1 Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
Analytical electrophoresis uses polyacrylamide gels to separate proteins without aggregation. It denature proteins using a reducing agent along with sodium dodecyl sulfate (SDS) as an anionic detergent, allowing separation based on molecular weight during electrophoresis [51]. SDS effectively denatures proteins by unfolding them and coating them in negatively charged SDS molecules. This masks the protein’s native charge. β-mercaptoethanol cleaves disulfide bonds. Uniformity in homology and charge to mass ration is attained after SDS and mercaptoethanol treatment of proteins. Electrophoretic mobility is determined by size, with smaller complexes moving faster due to the gel’s sieving effect. Mobility is inversely proportional to protein mass [52].