Interaction between glutathione and glutathione-S-transferase on dendron self-assembled controlled pore glass beads

Controlled pore glass beads were modified with a conical shaped dendron and interaction between immobilized glutathione on top of the dendron and glutathione-S-transferase (GST) in cell lysate was examined. SDS-PAGE chromatogram showed that the dendron modified beads were effective not only in binding the corresponding proteins such as GST and GST-fused proteins but also in suppressing the nonspecific binding of proteins. Dramatic increase of ligand utilization (ca. 30%) was observed in comparison with the conventional approaches. Molecular weight dependence of the beads is comparable to that of Sepharose 4B.