Abstract
AbstractA low mol. wt protein (S protein) which has a high affinity for endogenous polar lipid was isolated from wheat gluten, partially purified and compared electrophoretically with low mol. wt components of several previously studied wheat protein preparations. Mobilities of S protein components in acidic polyacrylamide gel electrophoresis (PAGE) were very close to those of the chloroform/methanol soluble low mol. wt proteins (CM proteins). A fraction of S protein separated by gel filtration chromatography on Sephadex G‐50 (S‐III protein) was almost identical to CM proteins by two‐dimensional electrophoresis. Bands with mobilities similar to those of S‐III protein were present in PAGE patterns of gliadin, the low mol. wt fractions IV and V obtained from gliadin by gel filtration chromatography on Sephadex G‐200, and the albumin/globulin fraction of flour prepared by the Osborne solubility fractionation. Because of its variable solubility S protein cannot be unambiguously classified according to the Osborne solubility classification of plant proteins.
Published Version
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