| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10550336 | Journal of Chromatography B | 2005 | 4 Pages |
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.
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Physical Sciences and Engineering
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Authors
Annelise Sahin, Emmanuel Tetaud, Gilles Merlin, Xavier Santarelli,