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Renatured (Commentary)
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2.5.1.31
the recombinant protein in the pellet is solubilized with 7 M urea and purified using nickel-nitrilotriacetic acid under denaturing conditions. The protein refolding is achieved via the stepwise dialysis to remove the denaturant in the presence of 6 mM beta-mercaptoethanol. Alternatively, on-column refolding is carried out in a single step to obtain the active protein in large quantities. beta-Mercaptoethanol and Triton are both required in this quick refolding process
637486
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