Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in <i>Escherichia coli</i>
抄録
<jats:p>There are many fusion protein systems now available for insoluble expression: TrpLE, ketosteroid isomerase, PurF, and PagP, for example. The ideal fusion partner is effective at directing a wide variety of target proteins into inclusion bodies, accumulates in large quantities in a highly pure form, and is readily solubilized and purified in commonly used denaturants. Fusion partner removal under denaturing conditions is biochemically challenging, requiring harsh conditions (e.g., cyanogen bromide in 70% formic acid) that can result in unwanted protein modifications. Recent advances in metal ion‐catalyzed peptide bond cleavage allow for more mild conditions, and some methods involving nickel or palladium will likely soon appear in more biological applications.</jats:p>
収録刊行物
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- FEBS Letters
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FEBS Letters 588 (2), 247-252, 2013-09-27
Wiley
