The acetic acid soluble proteins extracted from wheat flour have been separated into 11 fractions by a chromatographic procedure using columns of carboxymethyl- cellulose, equilibrated with O� 005M acetate buffer, pH 4�1. Under theso conditions one fraction passes unretarded through the column. Eight further fractions are eluted at pH 4� 1 by employing a gradient to O� 2M N aCl in the presence of 1M dimethyl formamide (DMF) which prevents protein precipitation at ionic strengths greater than 0�03.

SummarySeven fractions obtained from wheat gluten by chromatography on carboxy~ methyl-cellulose were studied by ultracentrifugation, gel electrophoresis, chemical, and N-terminal amino acid analysis. On rechromatography, five fractions eluted by sodium chloride behaved as distinct entities. illtracentrifuge experiments indicated that four of these were each undergoing rapid, reversible association. Several N-terminal amino acids were found in each of the fractions which, moreover, could be resolved by the gel technique into a number of electrophoretic bands, some bands being common to those of neighbouring fractions. Total nitrogen values showed the chromatographic samples to be essentially free from non-protein material.

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