ELECTROPHORETIC CHARACTERIZATION OF FRACTIONS COLLECTED FROM GLUTEN PROTEIN EXTRACTS SUBJECTED TO SIZE-EXCLUSION HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY

The electrophoretic analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE; reduced and unreduced) of fractions, co llected from a size exclusion-high performance liquid chromatography ( SE-HPLC) separation of gluten proteins using a column with pare size o f around 400 Angstrom, showed clear resolution for the seven elution r anges studied in two Australian bread wheat lines. Polymeric proteins - high molecular weight (HMW) glutenin subunits, low molecular weight (LMW) glutenin subunits, HMW albumins and some modified omega-gliadins - appeared exclusively in the region within the first peak of the chr omatogram (fractions 1 to 5), the limit being a region that resolved a s a small peak before the large peal; of gliadins and where some omega -gliadins eluted. A larger proportion of HMW glutenin subunits and B s ubunits contributed to polymer formation of higher molecular weight. T he polymer size decreased as the proportion of the other protein compo nents increased.