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 (14kDa 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 K(d) of 2.8x10(-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Suwannarangsee S,Moulis C,Potocki-Veronese G,Monsan P,Remaud-Simeon M,Chulalaksananukul Wdoi
10.1016/j.febslet.2007.08.062subject
Has Abstractpub_date
2007-10-02 00:00:00pages
4675-80issue
24eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00944-1journal_volume
581pub_type
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