Abstract
After reduction and aminoethylation, glutenin can be separated into four groups of proteins by fractional precipitation from 0.5 M acetic acid solution with Cu(NO 3) 2. Material precipitated by 0.0283 M Cu(NO 3) 2 accounts for 22% (w/w) of the glutenin and consists primarily of slow moving electrophoretic components. This fraction, which has an amino acid composition unlike other proteins from gluten, contains large amounts of glycine and tyrosine and low levels of histidine, methionine, valine and cysteine. The remaining fractions from glutenin resemble other gluten proteins more closely in composition. Gel permeation chromatography of the protein components from glutenin shows they have higher apparent molecular weights than gliadin.
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