INHERITANCE OF GLUTEN PROTEIN-COMPONENTS OF A HIGH-PROTEIN HARD RED SPRING WHEAT LINE DERIVED FROM TRITICUM-TURGIDUM VAR DICOCCOIDES - SEMIPREPARATIVE RP-HPLC, GEL-ELECTROPHORESIS, AND AMINO-ACID-COMPOSITION STUDIES

A high-protein hard red spring (HRS) wheat line (ND 643), derived from crosses with Triticum turgidum var. dicoccoides (a high-protein wild tetraploid) and the HRS wheats Len and RL 4352-1, was investigated for inheritance of its protein components. Protein fractions of a 70% ethanol extract (gliadin proteins) of meal samples were collected by semipreparative reversed-phase high-performance liquid chromatography (semiprep RP-HPLC). Polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS)-PAGE of the fractions from RP-HPLC showed that ND 643 inherited most of its gliadin components in the alpha- and beta-gliadin regions from T. t. dicoccoides. PAGE and SDS-PAGE of the fractions from an Osborne solubility fractionation procedure showed that ND 643 inherited most of its glutenin and residue proteins from Len and RL 4352-1. Quantitative data from the Osborne procedure showed that ND 643 contained significantly more gliadin and residue proteins per unit weight of sample than Len or RL 4352-1. ND 643 also seemed to retain a ratio of gliadin to total glutenin proteins similar to those of its HRS parents of good bread-making quality. Amino acid composition analyses of the fractions from RP-HPLC showed that ND 643 possessed proteins having compositions similar to those of its HRS parents.