Cereal Chem 64:168-172   |  VIEW ARTICLE

Gel Filtration Chromatography of Glutenin in Dissociating Solvents: Effect of Removing Noncovalently Bonded Protein Components on the Viscoelastic Character of Glutenin.

U. J. S. Prasada Rao and S. N. Nigam. Copyright 1987 by the American Association of Cereal Chemists, Inc. 

Glutenin was chromatographed on Sephadex G-200 using the solvent mixtures of acetic acid, guanidine- HCl, and cetyltrimethyl ammonium bromide; sodium dodecyl sulfate; and phenol, acetic acid, and water in succession. The first two of these three solvents dissociated about 27% protein from glutenin as low molecular weight protein. Removal of this protein by gel filtration gave a residual glutenin (sodium dodecyl sulfate [SDS]-glutenin) from which the third solvent was not able to dissociate any more protein. The residual glutenin could, therefore, be regarded as core glutenin in which all the subunits are probably bound by interpolypeptide disulfide bonds. Viscoelastograph measurements showed that the elastic recovery in residual glutenin (SDS-glutenin) was about half of the starting glutenin (AcOH-glutenin). Thus, the noncovalently bonded polypeptides (low molecular weight protein) increased the elastic character of glutenin. This increase may simply be a result of the increase in the molecular weight of glutenin following accretion of noncovalently bonded polypeptides by residual glutenin (SDS-glutenin).