Nucleic Acids Res. 1982 Mar 11;10(5):1741-54.

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

Tanaka S, Oshima T, Ohsue K, Ono T, Oikawa S, Takano I, Noguchi T, Kangawa K, Minamino N, Matsuo H.

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

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