Cereal Chem 66:397-401   |  VIEW ARTICLE

Inheritance of Gluten Protein Components of High-Protein Hard Red Spring Wheat Lines Derived from Triticum turgidum var. dicoccoides.

K. Khan, R. Frohberg, T. Olson, and L. Huckle. Copyright 1989 by the American Association of Cereal Chemists, Inc. 

Three hard red spring (HRS) wheat lines were derived from crosses with a high-protein donor, Triticum turgidum var. dicoccoides. The three experimental lines were higher in protein content (14.0% moisture basis) by up to 3.0 percentage points more than their HRS wheat parental genotypes. These lines also were higher in water absorption, wet gluten content, and loaf volume than the HRS parents. Polyacrylamide gel electrophoresis of gliadin proteins showed that all three experimental lines inherited protein components in the alpha- and beta-gliadin regions from T. t. dicoccoides. All three experimental lines were known to inherit the first three protein components of lowest mobility in the omega-gliadin region from one of the parents, RL4352-1 (a selection of Columbus for rust resistance), because these three components do not occur in the other parents, Len, Coteau, and T. t. dicoccoides. Reversed-phase high-performance liquid chromatography showed that all three lines inherited gliadin components from T. t. dicoccoides that eluted in the most hydrophobic region of the elution profile. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the high molecular weight subunits of glutenin showed that two of the lines had the same subunit composition (2*, 7+9, 5+10) as the HRS wheat parents. One of the lines contained the subunit composition 1, 7+9, and 5+10, but subunit 1 is not present in the parent varieties. The possibility of contamination or genetic recombination with respect to the appearance of subunit 1 is discussed.