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].