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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Production of recombinant human pancreatic secretory trypsin inhibitor by Escherichia coli.

A synthetic gene for human pancreatic secretory trypsin inhibitor (PSTI) was fused to the coding sequence for the amino-terminal 135 amino acid residues of human interferon-gamma (IFN-gamma) by interposing a methionine codon sequence, and the resulting hybrid gene was efficiently expressed in Escherichia coli cells. Recombinant human PSTI (rHu-PSTI) was separated from the IFN-gamma/PSTI fused protein by cleavage at the methionine residue with cyanogen bromide. Finally, rHu-PSTI was purified by affinity chromatography on a bovine trypsin-CH-Sepharose 4B column. The amino acid composition, partial amino-terminal sequence, disulfide formation, human trypsin inhibitory activity, and immunoreactivity against rabbit anti-human PSTI serum of rHu-PSTI corresponded to those of the natural form.[1]

References

  1. Production of recombinant human pancreatic secretory trypsin inhibitor by Escherichia coli. Kikuchi, N., Nagata, K., Horii, T., Miyazaki, S., Shin, M., Takimoto, N., Tsuruta, Y., Tamaki, M., Teraoka, H., Yoshida, N. J. Biochem. (1987) [Pubmed]
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