Three γ-gliadin components were separated and purified by reversed-phase and gel-permeation high-performance liquid chromatography after extraction from defatted wheat flour with 70% ethanol. The apparent relative molecular mass (M rs) of the components, termed 8A-1, 8A-2, and 8B were 38,000, 35,000 and 45,000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The purified components had amino acid compositions typical of γ-gliadins. Components 8A-1 and 8B were classified as γ 2- and γ 3-gliadins, respectively, on the basis of their N-terminal amino acid sequences. The circular dichroism spectrum of component 8 B indicated that it contained α-helical conformations (about 27%) and β-structures (about 32%); the spectrum was characteristic of an α+β type protein with separate α-helix- and β-sheet-rich regions.