Abstract
A panel of murine monoclonal antibodies (MAbs) was generated to the total glutenin fraction of wheat. Two of the MAbs (IFRN 0061 and 00614) were characterized in terms of their binding to cereal prolamins using immunoassay and immunoblotting techniques. Their specificities, as determined by immunoassay, were restricted, binding mainly to the S-poor prolamins of barley, wheat and rye, and they exhibited a high affinity for the major repeat motif, PQQPFPQQ, present in these polypeptides. Analysis of genetic stocks by immunoblotting showed that the epitopes recognized by these MAbs are present in the polymeric LMW subunits of glutenin encoded by genes on the short arms of the group 1 chromosomes of wheat.