Cereal Chem 44:611 - 619.  |  VIEW ARTICLE
Characterization of the Acetic Acid-Insoluble Fraction of Wheat Gluten Protein.

J. E. Cluskey and R. J. Dimler. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

The acetic acid-insoluble protein in wheat gluten was extracted in good yield by using a hydrochloric acid- 2-chloroethanol solvent after acetic acid extraction. The isolate was found by moving-boundary electrophoresis to have components with mobilities similar to those of glutenin and faster-moving protein. Starch-gel electrophoresis of the insoluble protein after reduction and alkylation demonstrated several components of high electrophoretic mobility similar to that of reduced water-soluble proteins, and lesser amounts of constituents resembling reduced glutenin. The amino acid composition of the insoluble protein was more like that of water-soluble proteins than like that of glutenin. The protein insoluble in acetic acid appears to be a mixture of high-molecular-weight constituents consisting in part of a variety of polypeptides intermolecularly linked together through disulfide bonds and resembling most closely those of the water- soluble proteins of the wheat flour.