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. 2019 Jul 27;11(8):689. doi: 10.3390/v11080689

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Purification of the FIV recombinant Pr50^Gag-His₆-tag protein from soluble fractions by immobilized metal affinity chromatography (IMAC) and its western blot analysis. (A) Coomassie Brilliant Blue-stained SDS-polyacrylamide gel on which bacterial soluble fractions containing FIV Pr50^Gag-His₆-tag fusion protein was electrophoresed before and after IMAC purification using different concentrations of immidazole. Western blot analyses on the same soluble fractions (before and after IMAC purification) using α-His₆ (B) and FIV α-p24 (C) monoclonal antibodies, respectively, using equal amounts of protein.