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- W1554934111 abstract "Publisher Summary This chapter describes the cloning, sequencing, and overexpression of the E. coli MsrA gene and large-scale purification of the protein. The purification is done essentially in one step, yielding milligram quantities of the biologically active protein. The additional glycine residue introduced at the N terminus, owing to genetic manipulations, does affect the catalytic activity of the enzyme. The observation that the fusion protein in the S30 extracts of XL1/pAR200 exhibited MsrA activity also shows that even a large addition to the N terminus of MsrA is without any major effect on its activity. The growth inhibition of E. coli cells after exposure to H 2 O 2 or OCl − can be partially reversed by transforming the cells with pAR100. The chapter demonstrates in vivo that oxidative damage in E. coli is, in part, because of the oxidation of methionine residues in protein and that MsrA can reverse this damage." @default.
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- W1554934111 date "1995-01-01" @default.
- W1554934111 modified "2023-09-25" @default.
- W1554934111 title "[45] Escherichia coli peptide methionine sulfoxide reductase: Cloning, high expression, and purification" @default.
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- W1554934111 doi "https://doi.org/10.1016/0076-6879(95)51150-4" @default.
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