Cereal Chem 69:270- 274   |  VIEW ARTICLE

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.

K. Khan, L. Huckle, and B. L. Jones. Copyright 1992 by the American Association of Cereal Chemists, Inc. 

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.