Cereal Chem 67:250-257   |  VIEW ARTICLE

Wheat Low Molecular Weight Glutenin Subunits---Structural Relationship to Other Gluten Proteins Analyzed Using Specific Antibodies.

J. H. Skerritt and L. G. Robson. Copyright 1990 by the American Association of Cereal Chemists, Inc. 

The immunological homologies of low molecular weight glutenin subunits (LMW-GS) were compared with the other major wheat gluten polypeptides, high molecular weight glutenin subunits (HMW-GS) and gliadins. Conventional one-dimensional polyacrylamide gel electrophoretic (PAGE) methods were used as well as a two-step, one-dimensional sodium dodecyl sulfate-PAGE technique, together with immunoblotting and enzyme-immunoassay methods. Many antibodies raised to gliadins and HMW-GS bound well to LMW- GS. Antibodies with specificities for similar groups of gliadins bound to similar groups of glutenins; some antibodies bound to each of the major gliadins, LMW-GS, and HMW-GS but not to other grain proteins, suggesting the existence of "common gluten" amino acid sequences or conformations. The solubility and immunochemical similarities as well as the known linkage between the genes for LMW-GS and certain gliadins mean that LMW-GS may be responsible for many biochemical properties and quality effects usually attributed to gliadins.