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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Production of a biologically active recombinant teleostean growth hormone in E. coli cells.

We have isolated and characterized several recombinant lambda phage clones carrying growth hormone ( GH) cDNA of striped bass (Morone saxatilis). Nucleotide sequence and the predicted amino acid sequence of sbGH was determined from a recombinant clone carrying the longest cDNA insert. The sbGH cDNA encodes a pre-hormone of 204 amino acid residues. Comparison of the predicted amino acid sequence of sbGH with those of other vertebrates revealed different degrees of sequence identity: approximately 98% with European sea bass; 90% with bluefin tuna; bonito and red seabream; 71% with winter flounder; 64% with salmonids; 55% with carp; and 38% with human. Expression of the mature sbGH cDNA (without the signal peptide sequence) in E. coli cells under regulation of the lambda phage PL promoter produced a polypeptide of 20 kDa. Following renaturation, this recombinant hormone was shown to be biologically active in a radioreceptor competition binding assay and in the induction of hepatic insulin-like growth factor I (IGF-I) mRNA synthesis in vivo.[1]


  1. Production of a biologically active recombinant teleostean growth hormone in E. coli cells. Cheng, C.M., Lin, C.M., Shamblott, M., Gonzalez-Villasenor, L.I., Powers, D.A., Woods, C., Chen, T.T. Mol. Cell. Endocrinol. (1995) [Pubmed]
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