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. 2012 Jun 24;13:11. doi: 10.1186/1471-2091-13-11

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Copyright ©2012 Sengottaiyan et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Purification of recombinant His₆-Gtr1 wild-type protein by immobilized metal affinity chromatography. Coomassie Brilliant Blue stained 12 % (w/v) acrylamide SDS gel containing following samples: M, prestained protein molecular weight marker (kDa); lane 1, aliquot of sonicated total cell lysate; lane 2, aliquot of soluble fraction of total cell lysate after centrifugation at 40,000 g; lane 3, flow-through protein from the Ni²⁺-NTA column, and lanes 4–9, eluted fractions of His₆-Gtr1 wild-type protein. Prior to the GTPase assay, an aliquot of eluted His₆- Gtr1 wild-type protein from the Ni²⁺-NTA column was verified by Western blot analysis (right panel) using anti-His antibody.