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Nucleic Acids Research, 1982, Vol. 10, No. 5 1741-1754
© 1982

MOLECULAR BIOLOGY

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

Shoji Tanaka, Takehiro Oshima, Kazuhiro Ohsue, Teiichi Ono, Shinzo Oikawa, Isamu Takano, Teruhisa Noguchi, Kenji Kangawa*, Naoto Minamino* and Hisayuki Matsuo*

Suntory Institute for Biomedical Research 1-1 Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618, Japan *Department of Biochemistry, Miyazaki Medical College Kihara, Kiyotake, Miyazaki 889-16, Japan

Received January 12, 1982. Accepted February 8, 1982.

Chemically synthesized {alpha}-neo-endorphin gene was fused to the Escherlchia coli ß-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 105 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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