AbstractStarch‐gel electrophoresis has shown that reduction of the glutenins of Cappelle, Conley, Elite and Wichita wheats causes a number of components to appear, some of which have mobilities equal to those of the corresponding reduced gliadin. Several other bands are found with mobilities close to those of bands in the reduced gliadin pattern. This evidence is consistent with a hypothesis of Woychik et al. that glutenin is built up chiefly from gliadin proteins. Varietal differences are observed when four glutenins, reduced under similar conditions, are compared. It seems likely that glutenin of low molecular weight can enter starch gels during electrophoresis and superimpose an artifact stain among gliadin bands unless precautions are taken to remove it. Defatting flour does not influence appreciably the quality of the electrophoretic pattern of the derived gliadin except that contamination by glutenin is greatly reduced. Some alteration of intensity distribution can, however, be brought about by defatting, probably due to varying solubilities in the lipid solvent. No evidence for the presence of lipoprotein was found in gliadin from undefatted flour.