• Title of article

    LdARL-1 His-tagged recombinant protein: purification by immobilized metal affinity expanded bed adsorption

  • Author/Authors

    Sahin، نويسنده , , Annelise and Tetaud، نويسنده , , Emmanuel and Merlin، نويسنده , , Gilles and Santarelli، نويسنده , , Xavier، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2005
  • Pages
    4
  • From page
    19
  • To page
    22
  • Abstract
    Previously we have cloned three ADP-ribosylation factor-like (ARL) genes from the parasitic protozoan Leishmania donovani: LdARL-3A and 3B, LdARL-1. LdARL-3A was previously purified as an active native form, which was able to bind GTP in vitro. In this paper, we have performed the production and the purification of Histidine-tagged (His-tagged) LdARL-1 recombinant protein by immobilized metal affinity chromatography (IMAC) using expanded bed adsorption (EBA) technology. This protein was purified with more than 95% purity and could be successfully used for GTP-binding assay.
  • Keywords
    LdARL-1 , ADP-ribosylation factor-like protein , His-tagged recombinant protein , Immobilized metal affinity chromatography (IMAC) , Expanded bed adsorption
  • Journal title
    Journal of Chromatography B
  • Serial Year
    2005
  • Journal title
    Journal of Chromatography B
  • Record number

    1457288