Patterns of seed proteins in Triticum monococcum (2n = 2x = 14 = AA), Aegilops ventricosa (2n = 4x = 28 = DDMVMV), and their synthetic amphiploid were studied. The distribution of proteins in the individual Osborne protein fractions of the amphiploid was characterized by a 14 per cent increase in the main reserve-protein group — the gliadins, with a concomitant decrease in the salt-soluble proteins and the glutenins. Also the amino-acid composition, especially of the gliadins, was influenced by the amphiploidy. The gliadins from T. monococcum had higher contents of histidine, arginine, aspartic acid, serine, and isoleucine than Ae. ventricosa. In the amphiploid the epistasis of Ae. ventricosa over T. monococcum in most morphological attributes was parallelled in the amino-acid composition of the Osborne protein fractions. Such parallelism may have evolutionary significance. The salt-soluble proteins of the amphiploid and the parental varieties were separated in two dimensions according to molecular weight by gel chromatography and according to electrical charge at pH 9.5 by disc electrophoresis. Epistasis of Ae. ventricosa was again manifested by the prevalence of major proteins from this species in the amphiploid. Similarities in the protein patterns of T. monococcum and Ae. ventricosa provided further evidence of homoeoallelism in the A, D, and MV genomes. In most instances, however, the amphiploid represented additiveness of the parental proteins, especially with regard to the gliadins.
|Publication status||Published - 1972|