Histone deacetylase complexes: functional entities or molecular reservoirs |
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Authors: | Khochbin S Kao H Y |
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Institution: | Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Equipe chromatine et expression des gènes, Institut Albert Bonniot, Faculté de Médecine, Domaine de la Merci, 38706 La Tronche Cedex, France. khochbin@ujf-grenoble.fr |
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Abstract: | 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 90% or better. The results suggest that DBD can be used as a powerful carrier for purification of various recombinant proteins. |
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Keywords: | Dextran Dextran-binding domain Glucosyltransferase Purification Recombinant protein Tag |
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