Gel isoelectric focusing of wheat alcohol dehydrogenase

Summary Alcohol dehydrogenase (ADH) of different hexaploid wheat subspecies and varieties was investigated by isoelectric focusing in polyacrylamide gels. With this technique six ADH isoenzymes can be separated, while by the standard electrophoretic technique only three are visible. The ADH pattern revealed by isoelectric focusing is in full accordance with the hypothesis that the active ADH isozymes in hexaploid wheat are dimers composed of six possible combinations of subunits coded by triplicate structural genes.