Reduction and starch-gel electrophoresis of wheat gliadin and glutenin

Reduction of the disulfide bonds of wheat gliadin and glutenin followed by electrophoresis in starch gel revealed the presence of some components which are perhaps common to both proteins. There were marked quantitative differences in the distribution of components. The release of 20 or more electrophoretic components from the previously unresolved glutenin fraction is further evidence that extensive intermolecular disulfide bonding is responsible for its high molecular weight. Intermolecular disulfide bonding is present only to a limited extent in the gliadin fraction.