Abstract
Gliadin proteins extracted from fifteen Chinese and Yugoslav winter wheat cultivars were fractionated using a new separation technique – Capillary Zone Electrophoresis (CZE). Different CZE conditions were defined to optimize resolution and reproducibility of gliadin separations. Excellent resolution and high reproducibility of gliadin CZE patterns were obtained by using 47 cm length, 50 μm i.d. capillaries at 15 kV and 30° C in sodium borate buffer system with acetonitrile (ACN) and sodium dodecyl sulfate. By using these CZE conditions, gliadin proteins from each cultivar were easily separated into more than 35 components. This resolution is generally superior to that of one- and two-dimensional electrophoresis and RH-HPLC. Analysis of reproducibility of gliadin CZE patterns from Chinese cultivar ‘Lumai 6’ showed that the average relative standard deviation (RSD) for peak migration times and heights was 0.21% and 4.06%, respectively. Gliadin electrophoregrams of all cultivars studied showed clear qualitative and quantitative differences, including presence or absence of some major peak, migration times and heights of peaks. Specifically, some closely related cultivars that were not differentiable by A-PAGE, were readily differentiated by CZE. In addition, winter wheat cultivars from China and Yugoslavia showed greater differences in gliadin compositions revealed by CZE.
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