A modified method for the purification of active large enzymes using the glutathione S-transferase expression system

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Abstract

The glutathione S-transferase (GST) fusion protein system is widely used for high-level expression and efficient purification of recombinant proteins from bacteria. However many GST-tagged proteins are insoluble, and the existing procedures, which employ a mixture of detergents to solubilize the molecules, frequently compromise their functional activity. A further limitation is that large proteins (>80 kDa) are poorly isolated by the current methods and are contaminated by truncated forms. To overcome these problems, we provide here an improved method for efficient purification of active large GST-tagged enzymes such as the 180-kDa GST-fused mitochondrial RNA polymerase.

Autore Pugliese

Tutti gli autori

  • ROBERTI M.;CANTATORE P.;LOGUERCIO POLOSA P.A.M.

Titolo volume/Rivista

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Anno di pubblicazione

2012

ISSN

0003-2697

ISBN

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Numero di citazioni Wos

Nessuna citazione

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Numero di citazioni Scopus

2

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Settori ERC

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Codici ASJC

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