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Synthesis of calf prochymosin (prorennin) in Escherichia coli.

A gene for calf prochymosin (prorennin) has been reconstructed from chemically synthesized oligodeoxyribonucleotides and cloned DNA copies of preprochymosin mRNA. This gene has been inserted into a bacterial expression plasmid containing the Escherichia coli tryptophan promoter and a bacterial ribosome binding site. Induction of transcription from the tryptophan promoter results in prochymosin synthesis at a level of up to 5% of total protein. The enzyme has been purified from bacteria by extraction with urea and chromatography on DEAE-cellulose and converted to enzymatically active chymosin by acidification and neutralization. Bacterially produced chymosin is as effective in clotting milk as the natural enzyme isolated from calf stomach.[1]

References

  1. Synthesis of calf prochymosin (prorennin) in Escherichia coli. Emtage, J.S., Angal, S., Doel, M.T., Harris, T.J., Jenkins, B., Lilley, G., Lowe, P.A. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
 
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