Intermolecular disulfide bonds link specific high-molecular-weight glutenin subunits in wheat endosperm. |
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Authors: | H P Tao A E Adalsteins D D Kasarda |
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Institution: | Western Regional Research Center, U.S. Department of Agriculture, Albany, CA 94710. |
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Abstract: | A detergent wash extracted soluble proteins from wheat flour, leaving a residue enriched with insoluble glutenin aggregates. Digestion of this residue with endoproteinase Lys-C, which showed a limited specificity for glutenin subunits, produced several peptides with apparent molecular weights close to those of intact high-molecular-weight glutenin subunits. N-terminal sequencing indicated that the isolated peptides were composed of high-molecular-weight glutenin subunit fragments joined by an intermolecular disulfide bond. In two of these peptides, only two components were found, one from an x-type subunit and the other from a y-type subunit. The isolated peptides all contained at least one x-type C-terminal region and one y-type N-terminal region, suggesting a specific orientation to the intermolecular disulfide linkage. |
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