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Preparative isoelectric focusing of reduced wheat gluten proteins
Author(s) -
Curioni Andrea,
Peruffo Angelo Dal Belin,
Pogorberto E.
Publication year - 1990
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.1150110605
Subject(s) - glutenin , isoelectric focusing , chemistry , polyacrylamide gel electrophoresis , chromatography , gel electrophoresis , isoelectric point , gluten , electrophoresis , urea , sodium dodecyl sulfate , dithiothreitol , two dimensional gel electrophoresis , gel electrophoresis of proteins , biochemistry , protein subunit , proteomics , gene , enzyme
Proteins extracted from gluten of the bread wheat cultivar Fiorello 2 in the presence of 2‐mercaptoethanol or dithiothreitol were separated by isoelectric focusing in a free solution in a pH 3–10 gradient containing 50% v/v 1‐propanol or urea. The collected fractions were analyzed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis in 10% gels (high and medium molecular weight glutenin subunits) and 16% gels (low molecular weight gliadins). The isoelectric focusing pattern of gluten polypeptides in 50% v/v 1‐propanol was comparable to that obtained on two‐dimensional gel electrophoresis, based on isoelectric focusing and polyacrylamide gel electrophoresis or nonequilibrium pH gradient electrophoresis and polyacrylamide gel electrophoresis. A similar isoelectric focusing pattern was also observed when 3M urea was used as solvent. New gluten polypeptides, similar in mobility to the high molecular weight subunits of glutenin were detected at acidic pH.