Reduced alkylated glutenin subunits from wheat flour were fractionated by preparative electrophoresis at acid pH. The high molecular weight glutenin subunits (HMW-GS) and some of the low molecular wight glutenin subunits (LMW-GS) were purified by this one-step procedure, whereas the remainder of the LMW-GS, comigrating in the acid system, were purified in a second step by electroendosmotic preparative electrophoresis in the presence of sodium dodecyl sulfate. The quantities of recovered protein were sufficient for biochemical characterization and/or antibody production.
Wheat glutenin subunits purification by preparative acid and two-dimensional electrophoresis
CURIONI, ANDREA;
1995
Abstract
Reduced alkylated glutenin subunits from wheat flour were fractionated by preparative electrophoresis at acid pH. The high molecular weight glutenin subunits (HMW-GS) and some of the low molecular wight glutenin subunits (LMW-GS) were purified by this one-step procedure, whereas the remainder of the LMW-GS, comigrating in the acid system, were purified in a second step by electroendosmotic preparative electrophoresis in the presence of sodium dodecyl sulfate. The quantities of recovered protein were sufficient for biochemical characterization and/or antibody production.
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