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Nucleic Acids Research, 1983, Vol. 11, No. 5 1283-1294
© 1983

MOLECULAR BIOLOGY

Expression of chemically synthesized {alpha}-neo-endorphin gene fused to E. coli alkaline phosphatase

Kazuhiro Ohsuye, Midori Nomura, Shoji Tanaka, Ichiro Kubota, Hiroshi Nakazato, Hideo Shinagawa*, Atsuo Nakata* and Teruhisa Noguchi

Suntory Institute for Biomedical Research, 1-1 Wakayamadai, Shimamoto-cho, Mishima-gun Osaka 618 *Department of Experimental Chemotherapy, The Research Institute for Microbial Diseases Osaka University, 3-1, Yamadaoka, Suita, Osaka 565, Japan

Received January 13, 1983. Accepted February 1, 1983.

An {alpha}-neo-endorphin ({alpha}NE) gene, which we previously synthesized chemically and inserted into E.coli (ß-galactosidase gene of pK013 plasmid, has been excised and fused to E.coli alkaline phosphatase (APase) gene. One of the transformants was named E15/pA{alpha}NEl. Under the APase gene regulation, APase-{alpha}NE chimeric protein was expressed at 1.3 x 106 molecules per cell, and accounted for about 60+ of total cellular proteins. The HPLC pattern of CNBr treated E15/pA{alpha}NEl was very simple reflecting the high content of the chimeric protein and low numbers of methionine residues in it.

A series of genes encoding APase-{alpha}NE chimeric proteins in which 30 to 94 C-terminal amino acid residues were replaced by (met)-{alpha}NE, was cloned in E.coli. Transportation of the chimeric proteins to periplasmic space was studied. All chimeric proteins were apparently processed by signal peptidase but few, if any, was transported to the periplasmic space.


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