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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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/130002
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