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Science 5 February 1982:
Vol. 215. no. 4533, pp. 687 - 689
DOI: 10.1126/science.7036343
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Articles

Science, Vol 215, Issue 4533, 687-689
Copyright © 1982 by American Association for the Advancement of Science

articles

Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins

DC Williams, RM Van Frank, WL Muth, and JP Burnett

Escherichia coli that has been genetically manipulated by recombinant DNA technology to synthesize human insulin polypeptides (A chain, B chain, or proinsulin) contains prominent cytoplasmic inclusion bodies. The amount of inclusion product within the cells corresponds to the quantity of chimeric protein formed by the bacteria. At peak production, the inclusion bodies may occupy as much as 20 percent of the Escherichia coli cellular volume.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Effects of novel peptides derived from the acidic tail of synuclein (ATS) on the aggregation and stability of fusion proteins.
S. M. Park, K. J. Ahn, H. Y. Jung, J. H. Park, and J. Kim (2004)
Protein Eng. Des. Sel. 17, 251-260
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Chloroplasts Can Accommodate Inclusion Bodies.
S. L. Ketchner, D. Drapier, J. Olive, S. Gaudriault, J. Girard-Bascou, and F.-A. Wollman (1995)
J. Biol. Chem. 270, 15299-15306
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Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors.
T. Wilson, R. Paulsen, K. Padgett, and J Milbrandt (1992)
Science 256, 107-110
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A specific ovarian tumor protein isoform is required for efficient differentiation of germ cells in Drosophila oogenesis..
W R Steinhauer and L J Kalfayan (1992)
Genes & Dev. 6, 233-243
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Rabies virus glycoprotein analogs: biosynthesis in Escherichia coli.
E Yelverton, S Norton, J. Obijeski, and D. Goeddel (1983)
Science 219, 614-620
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Protein engineering.
K. Ulmer (1983)
Science 219, 666-671
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