Folding of Eukaryotic Proteins Produced in Escherichia Coli

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Abstract
The development of recombinant DNA technology has allowed production in prokaryotic hosts of proteins derived from eukaryotic organisms. The use of heterologous expression has had a large impact on the pharmaceutical industry since it enables large scale production of proteins which may have been difficult to isolate from a natural source. This approach also avoids the potential for contamination with disease agents associated with the isolation of a protein from human tissues. An example of this approach is the production in Escherichia coli of human growth hormone (1), used in the treatment of pituitary dwarfism. Studies of protein structure-function are also facilitated if the target protein can be produced in a prokaryote. For these studies, heterologous expression enables rapid production of variant proteins, either by directed or random mutagenesis, in sufficient quantities for detailed characterization using biochemical and biophysical methods.