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
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
Journal title :
Journal of Chromatography B