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Using the dextran-binding domain (DBD) of a type of glucosyltransferase (GTF) from Streptococcus sobrinus, we have developed a novel method for purifying recombinant proteins. DBD-tagged green and red fluorescent proteins as well as the parent GTF and DBD moiety were adsorbed well to commercially available cross-linked dextran (such as Sephadex beads and Sephacryl beads), and eluted efficiently with water-soluble dextran. The purity of the eluted proteins after this one-step affinity purification was V90% or better. The results suggest that DBD can be used as a powerful carrier for purification of various recombinant proteins. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

A novel approach for purification of recombinant proteins using the dextran binding domain