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Purification of wheat glutenin subunits by preparative acid and two‐dimensional electrophoresis
Author(s) -
Curioni Andrea,
Morel MarieHélène,
Furegon Luca,
Redaelli Rita,
Peruffo Angelo Dal Belin
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601168
Subject(s) - glutenin , chemistry , sodium dodecyl sulfate , gel electrophoresis , chromatography , electrophoresis , biochemistry , polyacrylamide gel electrophoresis , protein subunit , enzyme , gene
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.