Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049571 | FEBS Letters | 2007 | 6 Pages |
Abstract
Fourteen truncated forms of Leuconostoc mesenteroides NRRL B512-F dextransucrase, involving N-, C- or N- plus C-terminal domain truncations were tested for their ability to bind dextrans. The shortest fragment (14 kDa molecular weight) that still exhibited a strong interaction with dextran was localized between amino acids N1397 and A1527 of the C-terminal domain (GBD-7) and consists of six YG repeats. With a dissociation constant Kd of 2.8 × 10−9 M, this motif shows a very high affinity for isomaltohexaose and longer dextrans, supporting the proposed role of GBD in polymer formation. The potential application of GBD-7 as an affinity tag onto cheap resins like Sephacryl® S300HR for rapid purification was evaluated and is discussed.
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Authors
Surisa Suwannarangsee, Claire Moulis, Gabrielle Potocki-Veronese, Pierre Monsan, Magali Remaud-Simeon, Warawut Chulalaksananukul,