The separation of glutenin from gluten proteins by the precipitation method was investigated with two kinds of wheat flours, Manitoba No. 2 and Western White. Glutenins separated by the pH-ionic strength method were purified by the repeated precipitation from 70% alcohol. ω-Gliadin contaminating the glutenin preparation separated by the pH-ionic strength method was removed effectively by the alcohol purification. On the other hand, contaminating γ-gliadin was not removed by this procedure. The γ-gliadin difficult to remove was characterized by both starch-gel and free boundaryelectrophoresis. Comparison of the purified glutenins was made with free boundary electrophoresis and ultraviolet absorption. No significant difference was observed between Manitoba No.2 and Western White.