Cereal Chem 56:63 - 67.  |  VIEW ARTICLE
Studies of Glutenin. XII. Comparison by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis of Unreduced and Reduced Glutenin from Various Iso lation and Purification Procedures.

K. Khan and W. Bushuk. Copyright 1979 by the American Association of Cereal Chemists, Inc. 

Glutenin was isolated from flour by several different published procedures. Examination of two crude glutenin preparations (modified Osborne acetic acid-soluble and 2-chloroethanol extract of residue protein) and four purified glutenin preparations, both in unreduced and reduced form, by sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE), showed that unreduced glutenin contains many protein components that enter the SDS-gel. These components correspond, in mobility, to many of the subunits of reduced glutenin identified by SDS-PAGE. A model of functional glutenin which includes subunits bound by noncovalent linkages is presented.