Cereal Chem 47:98 - 109.  |  VIEW ARTICLE
Analysis of Wheat Flour Proteins by Polyacrylamide Gel Electrophoresis.

J. M. Lawrence, H. E. Herrick, and D. R. Grant. Copyright 1970 by the American Association of Cereal Chemists, Inc. 

A method for estimating the actual amount of protein within each of various groups of wheat flour proteins of similar electrophoretic mobility has been described. The principal steps are 1) a single extraction of the flour with an aluminum lactate buffer of pH 3.2 containing 3M urea to solubilize as much as possible of the total protein; 2) addition of lysozyme as an internal standard; 3) electrophoresis at pH 3.2 in a 4% polyacrylamide gel containing 2.7M urea, which has been previously equilibrated with aluminum lactate by overnight electrophoresis; 4) dyeing the gels with 0.1% amido black dye in 7% acetic acid; 5) conversion of the color of the protein bands to graphical form by densitometry; 6) measurement of the peak areas by planimetry and conversion to actual concentration units through use of factors representing the dye-binding capacity of the various protein groupings. Some examples of results of application of the method to flours from several wheat varieties are given.