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  • Title: Metal-binding activity of the soluble recombinant pig metallothionein 1A expressed in Escherichia coli.
    Author: Sun D, Zhang H, Wu G, Zhu Q, Lv S, Guo D, Wu R, Bao J.
    Journal: Biol Trace Elem Res; 2012 Dec; 150(1-3):418-23. PubMed ID: 22760644.
    Abstract:
    Full-length cDNA for the pig metallothionein 1A (pMT1A) gene was synthesized based on the pig MT1A gene sequence in Genbank and cloned into the pMD18-T vector. After sequence analysis and structure prediction, the pMT1A gene was cloned into vector pET-32a (+) containing a His-tag. The recombinant pMT1A (rpMT1A) was expressed in a soluble form using Escherichia coli Rosetta™ (DE3) plysS cells. Western blotting showed that the purified rpMT1A protein bound an anti-His-tag monoclonal antibody. Further investigation revealed that the rpMT1A protein showed high metal-binding activity with the divalent metal ions copper (Cu²⁺), zinc (Zn²⁺), and cadmium (Cd²⁺).
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