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Protein Production By Stationary Phase Induction (Spi)

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An alternative method for expressing the recombinant proteins in Escherichia coli is proposed. Unlike the ordinary induction protocol where the cells in the early- to mid-log phase are induced for the protein production, this alternative protocol utilizes the cells in the stationary phase. By using a glutathione S-transferase fusion protein as an example, the protocol proposed in this report yielded a higher amount of the desired protein than that from the ordinary protocol. This protocol also suppressed the proteolytic cleavage of the desired protein in the Escherichia coli cytoplasm, thus it should be particularly useful to produce proteins that undergo unwanted cleavages.

Keywords: escherichia coli; glutathione; s-transferase; stationary phase induction (Spi)

Document Type: Review Article


Affiliations: Department of Applied Chemistry and Recombinant Protein Expression Center (RPEC) Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul, Korea 143-747

Publication date: 2003-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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