Abstract
We report the construction of modified highMrglutenin subunit genes with variable lengths of the repetitive domain and their expression inEscherichia coli. The modified glutenin subunits showed anomalously slow migration by SDS–PAGE characteristic of these polypeptides. Changes in the size of the repetitive domain correlated with both the migration behaviour on SDS–PAGE and with the surface hydrophobicities of the polypeptides measured by RP–HPLC. These constructs made it possible to obtain direct evidence for the first time that the anomalous electrophoretic mobilities of highMrglutenin subunits in SDS–PAGE, compared with globular proteins, are mainly due to the repetitive domain. These constructs should be useful for establishing the role of the repetitive domain of highMrglutenin subunits in determining the viscoelastic properties of dough. They also offer the possibility of creating new genetic variability for wheat improvement.
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