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Cereal Chem 60:379 - 380.  |  VIEW ARTICLE
Lipid-Mediated Aggregation of Gliadin.

F. Bekes, U. Zawistowska, and W. Bushuk. Copyright 1983 by the American Association of Cereal Chemists, Inc. 

Gliadins from undefatted and completely defatted flour were fractionated by gel filtration chromatography on a Sephadex G-200 column. Fraction I (excluded) from undefatted flour contained almost all of the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) subunits of the original unfractionated gliadin. After removal of lipids from this fraction, its protein was resolved into five peaks (fractions) on rechromatography on Sephadex G-200. The five protein fractions of the gliadin from defatted flour were reconstituted with the original lipids and chromatographed on Sephadex G-200. SDS-PAGE showed that the subunit composition of fraction I was similar to that of the original gliadin from undefatted flour. It was concluded that the lipid-mediated aggregation of high and low molecular weight subunits of gliadin is reversible.

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