Abstract
Proteins from wheat endosperm protein bodies were fractionated by SDS-polyacrylamide gel electrophoresis and electroblotted on to nitrocellulose membranes. The electroblotted proteins were incubated with biotin-labelled lectins having different sugar specificities. A number of lectins bound to the electroblotted proteins, and the specificities of the binding sites were tested using sugar inhibitors complementary to each of the lectins. The binding of the lectin from wheat germ (wheat germ agglutinin) was readily inhibited by low concentrations of a complementary trisaccharide sugar N,N′,N″ triacetylchitotriose, suggesting the presence of N-acetyl glucosaminecontaining glycoproteins in wheat storage proteins. Acid hydrolysis of mature wheat, reduced gluten proteins and subsequent chromatography failed to show the presence of D-glucosamine. The general electroblotting technique has shown lectins to be useful probes for groups of wheat polypeptides and indicates their potential usefulness in the affinity purification of wheat proteins.
Published Version
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