The high molecular weight glutenin subunits of wheat endosperm migrate
anomalously in sodium dodecyl sulfate (SDS) polyacrylamide gel electr
ophoresis. This anomolous migration was studied by capillary electroph
oresis employing an entangled polymer solution that contained SDS. The
nonrigid solution nature of the sieving matrix allowed for the easy p
reparation of the different matrix concentrations required for the con
struction of a Ferguson plot. A Ferguson plot analysis of these protei
ns suggested that the high molecular weight glutenin subunits possesse
d frictional coefficients similar to those determined for standard pro
teins of the same size, indicating that anomalous migration in polyacr
ylamide gels was due to decreased binding of SDS and not to a unique s
tructural conformation in the presence of SDS.