Hexaploid derivatives of wild emmer wheat (Triticum dicoccoides Koern.) were examined by electrophoresis for high molecular weight (HMW) glutenin subunits and for gliadin composition from 10 days after anthesis to full maturity. Two established bread wheats were included in the investigation for comparison. No outstanding or consistent differences were observed in the patterns of protein development between the wild emmer derivatives and the established bread wheats. HMW glutenin subunits were detectable in some of the wheats from 15 days after anthesis. Gliadins were detectable over the whole mobility range from 10 to 15 days after anthesis, although differences were observed between gliadin patterns produced by urea extraction compared with ethanol extraction. Nitrogen fertilisation resulted in a general increase in the intensity of protein patterns, but no major change in the relative intensity of components was apparent.