Abstract
Wheat-germ agglutinin is located only in the embryo of a dry wheat seed and not in the endosperm tissue. This distribution remains unaltered for up to 96 h of germination and growth. The lectin is found not only in a freely soluble form but also in reversible association with particulate subcellular components. There appear to be no polypeptides that can be solubilized with sonication and aqueous buffers from the embryo tissue that can interact with the agglutinin. In vivo, the lectin apparently remains uncomplexed to endogenous glycoconjugates or is only able to bind to glycosylated integral membrane polypeptides. Alternatively the potential endogenous receptor(s) to wheat-germ agglutinin may not contain a polypeptide. Although the lectin is not present in the endosperm, 7 polypeptides able to interact in a reversible way with wheat-germ agglutinin could be purified from that tissue.