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Protein Engineering vol. 1 no. 6 pp. 487-492, 1987
© 1987 Oxford University Press

OTHER

Efficient cleavage by {alpha}-thrombin of a recombinant fused protein which contains insulin-like growth factor I

Satoshi Nishikawa, Faculty of Pharmaceutical Sciences, Kohichi Yanase, Faculty of Pharmaceutical Sciences, Tomoko Tokunaga-Doi, Faculty of Pharmaceutical Sciences, Kazumi Kodama, Faculty of Pharmaceutical Sciences, Hideyuki Gomi, Faculty of Pharmaceutical Sciences, Seiichi Uesugi, Faculty of Pharmaceutical Sciences, Eiko Ohtsuka, Faculty of Pharmaceutical Sciences2, Yukio Kato, Faculty of Pharmaceutical Sciences1, Fujio Suzuki1 and Morio Ikehara

1Department of Biochemistry and Calcified-Tissue Metabolism, Faculty of Dentistry, Osaka University Osaka 565 2Hokkaido University Sapporo 060, Japan Osaka University Osaka 565

The gene for insulin-like growth factor I (IGF-I) was constructed from chemically synthesized deoxyoligonucleotides and expressed in Escherichia coli, under the control of a trp promoter, as a set of fusion proteins which were connected with a portion of human growth hormone through the recognition sequence for a sequence-specific protease, either blood coagulation factor Xa or {alpha}-thrombin. Upon induction with 3-indoleacrylic acid, fusion proteins accumulated with a yield of 10–30% of the total protein. A fusion protein connected through a tetradecapeptide (Asp-Asp-Pro-Pro-Thr-Val-Glu-Leu-Gln-Gly-Leu-Val-Pro-Arg) was efficiently and correctly cleaved by {alpha}-thrombin, and the purified IGF-I possessed somatomedin-like activity, as determined by the enhancement of sulfation of glycosaminoglycans in cultured costal chondrocytes from rabbits.

Keywords: fusion protein/gene expression in E.coli/insulin-like growth factor I (IGF-I)/synthetic gene/{alpha}-thrombin

Received September 16, 1987; revised November 10, 1987;
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