Abstract
A precipitating fraction was separated from glutenin dispersed in 0.01M acetic acid by ultracentrifugation. In starch gel electrophoresis after reduction and cyanoethylation this fraction gave the same pattern as the supernatant fraction of glutenin. However, gel filtration revealed that it was rich in components eluted in the void volume. The components were so aggregative that they could be separated by ultracentrifugation from reduced and cyanoethylated glutenin dispersed in 0.1M acetic acid. In amino acid analysis the aggregative components obtained by ultracentrifugation showed low contents of glutamic acid and proline and high contents of basic amino acids in comparison with usual glutenin. These results and the N-terminal amino acid analysis strongly suggested that the aggregative polypeptides were identical with Fraction P described by Mita et al., (1) which formed zonal precipitate in isoelectric focusing even in the presence of 6M urea. The content of aggregative components in glutenin was determined to be about 8%. They may contribute to the association of glutenin molecules to produce an influence on rheological properties of wheat dough.
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