Cereal Chem 40:110 - 120. | VIEW
Proteins of Wheat and Flour. The Separation and Purification of the Pyrophosphate-Soluble Proteins of Wheat Flour by Chromatography on DEAE-Cellulose.
D. H. Simmonds. Copyright 1963 by the American Association of Cereal Chemists, Inc.
Extraction of mature wheat flour with 0.01M sodium pyrophosphate at pH 7 yields a solution containing the albumin and globulin protein components, together with pentosan-protein and nucleoprotein fractions. Chromatography of this solution on diethylaminoethyl-cellulose (DEAE-cellulose) has now been improved to yield eight subfractions. Three of these peaks, D, E, and F, eluted by a gradient of increasing sodium chloride concentration, have been rechromatographed on a large scale on DEAE-cellulose to yield symmetrical elution patterns. When purified, these components also gave symmetrical electrophoretic patterns showing only small amounts of cross-contamination. Determination of the amino acid residues occupying the N-terminal position by Sanger's DNP-technique showed that peaks D and E contained serine only and peak F contained serine and threonine as N-terminal amino acid residues. A comparison of the elution patterns from DEAE- cellulose of the pyrophosphate extracts of ten different flours showed a marked difference in the relative amounts of the various components present.