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. 1982 Mar 11;10(5):1741–1754. doi: 10.1093/nar/10.5.1741

Expression in Escherichia coli of chemically synthesized gene for a novel opiate peptide alpha-neo-endorphin.

S Tanaka, T Oshima, K Ohsue, T Ono, S Oikawa, I Takano, T Noguchi, K Kangawa, N Minamino, H Matsuo
PMCID: PMC320563  PMID: 6280156

Abstract

Chemically synthesized alpha-neo-endorphin gene was fused to the Escherichia coli beta-galactosidase gene on the plasmid pKO13. The resulting recombinant DNA was used to transform E. coli cells. Radioimmunoassay for alpha-neo-endorphin in CNBr-treated bacterial cells showed that alpha-neo-endorphin was synthesized at approximately 5 x 10(5) molecules per single E. coli cell. One of the transformants, WA802/p alpha NE2, was used for alpha-neo-endorphin purification. From 10.9 g of wet cells, we isolated 4 mg of chemically pure and biologically active alpha-neo-endorphin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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