High level expression and purification of peptide methionine sulfoxide reductase in Escherichia coli - PubMed (original) (raw)
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- PMID: 1468111
High level expression and purification of peptide methionine sulfoxide reductase in Escherichia coli
M A Rahman et al. Cell Mol Biol. 1992 Aug.
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- Cell Mol Biol 1992 Sep;38(6):615
Abstract
The enzyme peptide methionine sulfoxide reductase catalyzes the conversion of methionine sulfoxide residues in proteins to methionine. The 636 nucleotide coding region of the peptide methionine sulfoxide reductase gene has been amplified from a genomic clone using the polymerase chain reaction and the product was subcloned into plasmid pGEX-2T downstream of the glutathione S-transferase gene under control of the tac promoter. Escherichia coli XL1-Blue cells transformed with this plasmid and induced with isopropylthio-beta-galactoside expressed high levels of the fusion protein. The protein was soluble and was purified to homogeneity by affinity binding to a glutathione-agarose resin followed by cleavage of the fusion protein with thrombin. Both the fusion protein and the purified peptide methionine sulfoxide reductase protein showed high peptide methionine sulfoxide reductase activity.
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