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Protein Engineering vol. 1 no. 1 pp. 17-21, 1986
© 1986 Oxford University Press

RESEARCH-ARTICLE

Expression of the amino terminal part of synthetic human growth hormone gene and somatomedin-like activity of expressed protein

T. Doi, T. Tokunaga, E. Ohtsuka1, Y. Hiraki2, F. Suzuki2 and M. Ikehara

Faculty of Pharmaceutical Science. Osaka University 1–6 Yamadaoka Suita, Osaka 565, Japan 1Hokkaido University Sapporo 060, Japan 2Department of Biochemistry and Calcified-Tissue Metabolism, Faculty of Dentistry, Osaka University 1–8 Yamadaoka Suita, Osaka 565, Japan

We have constructed three different plasmids containing parts of the human growth hormone gene using chemically synthesized oligomers and cloned them for the purpose of expressing them in Escherichia coli. AB, B and BC gene segments corresponding to ABhGH (residue 1–138), BhGH (residue 44–138) and BChGH (residue 44–192) were placed under the control of a tryptophan promoter in the expression vector. Upon induction with 3-indolylacrylic acid, ABhGH accumulated in cells but the BhGH and BChGH segments were not detected appreciably. Northern blotting analysis showed that the amount of mRNA transcribed from the AB gene segment was about ten-fold higher than that from the B or BC gene segment. ABhGH was found to have insulin-like growth factor I (IGF-I) activity, which could be explained by the hydrophilicity curves of these proteins.

Keywords: gene expression/messenger RNA structure/partial gene expression/protein hydrophilicity

Received June 6, 1986;
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