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Protein Expr Purif. 1999 Feb;15(1):77-82.

Disulfide bond formation and folding of plant peroxidases expressed as inclusion body protein in Escherichia coli thioredoxin reductase negative strains.

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  • 1Institute of Molecular Biology, University of Copenhagen, Oster Farimagsgade 2A, Copenhagen K, DK-1353, Denmark.


Escherichia coli is widely used for the production of proteins, which are of interest in structure and function studies. The folding yield of inclusion body protein is, however, generally low (a few percent) for proteins such as the plant and fungal peroxidases, which contain four disulfide bonds, two Ca2+ ions, and a heme group. We have studied the expression yield and folding efficiency of (i) a novel Arabidopsis thaliana peroxidase, ATP N; and (ii) barley grain peroxidase, BP 1. The expression yield ranges from 0 to 60 microgram/ml of cell culture depending on the peroxidase gene and the vector/host combination. The choice of E. coli strain in particular affects the yield of active peroxidase obtained in the folding step. Thus, the yield of active ATP N peroxidase can be increased 50-fold by using thioredoxin reductase negative strains, which facilitate the formation of disulfide bonds in inclusion body protein.

Copyright 1999 Academic Press.

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