Cereal Chem 46:470 - 477.  |  VIEW ARTICLE
Polyacrylamide-Gel Electrophoresis of Reduced and Alkylated Soybean Trypsin Inhibitors.

A. C. Eldridge and W. J. Wolf. Copyright 1969 by the American Association of Cereal Chemists, Inc. 

Polyacrylamide-gel electrophoresis of native and reduced-alkylated soybean trypsin inhibitors showed them to be different proteins rather than intramolecular disulfide forms or intermolecular disulfide polymers of a single protein. Reduction alone or reduction followed by alkylation caused one of the inhibitors to migrate much slower in 8M urea than did the native inhibitor. This decrease in mobility, which was accompanied by an increase in intrinsic viscosity, is attributed to an unfolding after cleavage of the disulfide cross-linkages.